ナショナルバイオリソースプロジェクト
-Barley Genetic Resources Database-
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| Clone Name | rbags30m08 |
|---|---|
| Clone Library Name | barley_pub |
>DLDH_SYNY3 (P72740) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (LPD) Length = 473 Score = 113 bits (282), Expect = 6e-25 Identities = 56/86 (65%), Positives = 67/86 (77%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 VS KT FK N+KALAE E DGIAK++YR DTGE+LG HI+G+HA+DLI EA+ AIA Sbjct: 387 VSTAKTYFKGNSKALAEKETDGIAKVVYRQDTGELLGAHIIGIHASDLIQEAAQAIADRK 446 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 ++EL VHAHPTLSEVLDE +K A Sbjct: 447 SVRELAFHVHAHPTLSEVLDEAYKRA 472
>DLDH1_BACST (P11959) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) Length = 470 Score = 69.7 bits (169), Expect = 7e-12 Identities = 35/86 (40%), Positives = 51/86 (59%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V K F AN +ALA N+ DG K++ R + G I+G I+G +A+D+I E AI G Sbjct: 375 VIAAKFPFAANGRALALNDTDGFLKLVVRKEDGVIIGAQIIGPNASDMIAELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 TAEDIALTIHAHPTLGEIAMEAAEVA 460
>DLDH2_PSEPU (P31052) Dihydrolipoamide dehydrogenase (EC 1.8.1.4) (E3 component| of 2-oxoglutarate dehydrogenase complex) (LPD-GLC) (Dihydrolipoamide dehydrogenase) (Glycine oxidation system L-factor) Length = 477 Score = 69.3 bits (168), Expect = 1e-11 Identities = 38/97 (39%), Positives = 56/97 (57%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V+V F A+ +A+A N+ G K+I T +LGVH++G AA+L+ + + A+ GT Sbjct: 379 VNVGTFPFAASGRAMAANDTGGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIAMEFGT 438 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAKVNSGVSHSVN 375 ++L + V +HPTLSE L E A VN G H N Sbjct: 439 SAEDLGMMVFSHPTLSEALHE--AALAVNGGAIHVAN 473
>DLDH1_BACSU (P21880) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (S complex, 50 kDa subunit) Length = 470 Score = 67.4 bits (163), Expect = 4e-11 Identities = 34/86 (39%), Positives = 50/86 (58%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K F AN +AL+ NE DG K+I R + G ++G I G A+D+I E S AI G Sbjct: 376 IVAAKFPFAANGRALSLNETDGFMKLITRKEDGLVIGAQIAGASASDMISELSLAIEGGM 435 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ + +HAHPTL E+ E + A Sbjct: 436 TAEDIAMTIHAHPTLGEITMEAAEVA 461
>DLDH2_BACSU (P54533) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| branched-chain alpha-keto acid dehydrogenase complex) (LPD-Val) (Dihydrolipoamide dehydrogenase) Length = 474 Score = 67.0 bits (162), Expect = 5e-11 Identities = 37/86 (43%), Positives = 47/86 (54%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + K F A KAL E DG K++ DT +ILGVH++G H D+I EA A L Sbjct: 382 VKIGKFPFMAIGKALVYGESDGFVKIVADRDTDDILGVHMIGPHVTDMISEAGLAKVLDA 441 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 E+ +H HPTLSE + E AA Sbjct: 442 TPWEVGQTIHPHPTLSEAIGEAALAA 467
>DLDH_PEA (P31023) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Glycine cleavage system L protein) (Dihydrolipoamide dehydrogenase) Length = 501 Score = 65.9 bits (159), Expect = 1e-10 Identities = 32/79 (40%), Positives = 50/79 (63%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A A + +G+ K+I +T +ILGVHI+ +A +LIHEA+ A+ Sbjct: 411 VGKFPFMANSRAKAIDNAEGLVKIIAEKETDKILGVHIMAPNAGELIHEAAIALQYDASS 470 Query: 479 QELKLAVHAHPTLSEVLDE 423 +++ HAHPT+SE + E Sbjct: 471 EDIARVCHAHPTMSEAIKE 489
>DLDH_PSEFL (P14218) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 477 Score = 65.5 bits (158), Expect = 1e-10 Identities = 36/97 (37%), Positives = 55/97 (56%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V+V F A+ +A+A N+ G+ K+I T +LGVH++G AA+L+ + + + GT Sbjct: 379 VNVGTFPFAASGRAMAANDTTGLVKVIADAKTDRVLGVHVIGPSAAELVQQGAIGMEFGT 438 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAKVNSGVSHSVN 375 ++L + V +HPTLSE L E A VN H N Sbjct: 439 SAEDLGMMVFSHPTLSEALHE--AALAVNGHAIHIAN 473
>DLDH_SCHPO (O00087) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (DLDH) (Dihydrolipoamide dehydrogenase) Length = 511 Score = 65.1 bits (157), Expect = 2e-10 Identities = 32/79 (40%), Positives = 47/79 (59%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 F AN++A + DG+ K+I +T +LGVH++G A +LI EA+ A+ G +++ Sbjct: 425 FSANSRAKTNMDADGLVKVIVDAETDRLLGVHMIGPMAGELIGEATLALEYGASAEDVAR 484 Query: 464 AVHAHPTLSEVLDELFKAA 408 HAHPTLSE E AA Sbjct: 485 VCHAHPTLSEATKEAMMAA 503
>DLDH_MACFA (Q60HG3) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Dihydrolipoamide dehydrogenase) Length = 509 Score = 64.3 bits (155), Expect = 3e-10 Identities = 32/91 (35%), Positives = 51/91 (56%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A + DG+ K++ + T +LG HILG A ++++EA+ A+ G Sbjct: 418 VGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASC 477 Query: 479 QELKLAVHAHPTLSEVLDELFKAAKVNSGVS 387 +++ HAHPTLSE E AA ++ Sbjct: 478 EDIARVCHAHPTLSEAFREANLAASFGKSIN 508
>DLDH_HUMAN (P09622) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) Length = 509 Score = 64.3 bits (155), Expect = 3e-10 Identities = 32/91 (35%), Positives = 51/91 (56%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A + DG+ K++ + T +LG HILG A ++++EA+ A+ G Sbjct: 418 VGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASC 477 Query: 479 QELKLAVHAHPTLSEVLDELFKAAKVNSGVS 387 +++ HAHPTLSE E AA ++ Sbjct: 478 EDIARVCHAHPTLSEAFREANLAASFGKSIN 508
>DLDH_CANFA (P49819) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Dihydrolipoamide dehydrogenase) Length = 509 Score = 64.3 bits (155), Expect = 3e-10 Identities = 32/91 (35%), Positives = 51/91 (56%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A + DG+ K++ + T +LG HILG A ++++EA+ A+ G Sbjct: 418 VGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHILGPGAGEMVNEAALALEYGASC 477 Query: 479 QELKLAVHAHPTLSEVLDELFKAAKVNSGVS 387 +++ HAHPTLSE E AA ++ Sbjct: 478 EDIARVCHAHPTLSEAFREANLAASFGKSIN 508
>DLDH_PIG (P09623) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Dihydrolipoamide dehydrogenase) Length = 509 Score = 63.9 bits (154), Expect = 4e-10 Identities = 32/91 (35%), Positives = 51/91 (56%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A + DG+ K++ + T +LG HI+G A ++I+EA+ A+ G Sbjct: 418 VGKFPFAANSRAKTNADTDGMVKILGQKSTDRVLGAHIIGPGAGEMINEAALALEYGASC 477 Query: 479 QELKLAVHAHPTLSEVLDELFKAAKVNSGVS 387 +++ HAHPTLSE E AA ++ Sbjct: 478 EDIARVCHAHPTLSEAFREANLAASFGKAIN 508
>DLDH_RHOCA (P95596) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 454 Score = 63.9 bits (154), Expect = 4e-10 Identities = 34/79 (43%), Positives = 44/79 (55%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K SF N +A A + +G K++ T ILG HI+G A D+IHE A+ G Sbjct: 364 VGKFSFMGNGRAKAVFQAEGFVKILADAATDRILGAHIIGPSAGDMIHEICVAMEFGASA 423 Query: 479 QELKLAVHAHPTLSEVLDE 423 Q+L L HAHPT SE + E Sbjct: 424 QDLALTCHAHPTYSEAVRE 442
>DLDH_CHLVI (O50311) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 469 Score = 63.2 bits (152), Expect = 7e-10 Identities = 35/91 (38%), Positives = 52/91 (57%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V ++ F A+ KA A + +G K+++ +TG++LG H++G A +LI E A G Sbjct: 379 VLVGRSQFAASGKANAYGQLEGFVKLVFNAETGKMLGGHLIGHDAVELIGELGLACRYGV 438 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAKVNSG 393 + L VHAHPTLSE + E +A N G Sbjct: 439 TAEGLVGTVHAHPTLSETVREAAFSALPNKG 469
>DLDH_AZOVI (P18925) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) Length = 477 Score = 62.4 bits (150), Expect = 1e-09 Identities = 34/90 (37%), Positives = 51/90 (56%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 F A+ +A+A N+ G K+I T +LGVH++G AA+L+ + + A+ GT ++L + Sbjct: 387 FAASGRAMAANDTAGFVKVIADAKTDRVLGVHVIGPSAAELVQQGAIAMEFGTSAEDLGM 446 Query: 464 AVHAHPTLSEVLDELFKAAKVNSGVSHSVN 375 V AHP LSE L E A V+ H N Sbjct: 447 MVFAHPALSEALHE--AALAVSGHAIHVAN 474
>DLDH_MOUSE (O08749) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Dihydrolipoamide dehydrogenase) Length = 509 Score = 62.4 bits (150), Expect = 1e-09 Identities = 31/82 (37%), Positives = 47/82 (57%) Frame = -1 Query: 653 KTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQE 474 K F AN++A + DG+ K++ T +LG HILG A ++++EA+ A+ G ++ Sbjct: 420 KFPFAANSRAKTNADTDGMVKILGHKSTDRVLGAHILGPGAGEMVNEAALALEYGASCED 479 Query: 473 LKLAVHAHPTLSEVLDELFKAA 408 + HAHPTLSE E AA Sbjct: 480 IARVCHAHPTLSEAFREANLAA 501
>DLDH_RHIET (O05940) Probable dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3| component of pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) (ORF-E3) (Fragment) Length = 277 Score = 61.2 bits (147), Expect = 3e-09 Identities = 32/81 (39%), Positives = 47/81 (58%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + V + SF AN KA+A E G+ K+I+ TGE+LG H++G +LI A+ L T Sbjct: 188 IRVGRFSFAANRKAIALGEDQGMVKVIFDKKTGELLGAHMVGAEVTELIQGFVVAMNLET 247 Query: 485 RLQELKLAVHAHPTLSEVLDE 423 +EL + HPT+SE + E Sbjct: 248 TEEELMHTIFPHPTVSETMKE 268
>DLDH2_HALMA (Q5UYG6) Dihydrolipoyl dehydrogenase 2 (EC 1.8.1.4)| (Dihydrolipoamide dehydrogenase 2) Length = 472 Score = 60.8 bits (146), Expect = 3e-09 Identities = 30/79 (37%), Positives = 47/79 (59%) Frame = -1 Query: 641 KANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLA 462 +AN +AL NE +G +++ D +LG I+G A++LI E I +G RL+++ Sbjct: 387 RANGRALTVNEKEGFVRVVADADEEFLLGAQIVGPEASELIAELGLGIEMGARLEDIAGT 446 Query: 461 VHAHPTLSEVLDELFKAAK 405 +H HPTLSE + E AA+ Sbjct: 447 IHTHPTLSEAVHEAAAAAR 465
>DLDH_CHLTR (O84561) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 465 Score = 60.8 bits (146), Expect = 3e-09 Identities = 34/81 (41%), Positives = 47/81 (58%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K F+A KA+A E DG A +I T +ILG +++G HA+ LI E + A+ Sbjct: 368 VKVTKFPFRAIGKAVAMGEADGFAAIISHETTQQILGAYVIGPHASSLISEITLAVRNEL 427 Query: 485 RLQELKLAVHAHPTLSEVLDE 423 L + +HAHPTL+EV E Sbjct: 428 TLPCIYETIHAHPTLAEVWAE 448
>DLDH_YEAST (P09624) Dihydrolipoyl dehydrogenase, mitochondrial precursor (EC| 1.8.1.4) (Dihydrolipoamide dehydrogenase) Length = 499 Score = 60.5 bits (145), Expect = 4e-09 Identities = 31/82 (37%), Positives = 45/82 (54%) Frame = -1 Query: 653 KTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQE 474 K F AN++A + +G K++ T ILG HI+G +A ++I EA A+ G ++ Sbjct: 411 KFPFAANSRAKTNQDTEGFVKILIDSKTERILGAHIIGPNAGEMIAEAGLALEYGASAED 470 Query: 473 LKLAVHAHPTLSEVLDELFKAA 408 + HAHPTLSE E AA Sbjct: 471 VARVCHAHPTLSEAFKEANMAA 492
>DLDH3_HALMA (Q5UWH2) Dihydrolipoyl dehydrogenase 3 (EC 1.8.1.4)| (Dihydrolipoamide dehydrogenase 3) Length = 477 Score = 60.5 bits (145), Expect = 4e-09 Identities = 28/80 (35%), Positives = 49/80 (61%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 F+A+ +AL N +G ++I +T ++G I+G A++LI E + I +G +L+++ Sbjct: 390 FQASGRALTANRAEGFVRIIATKETERVIGAQIVGPEASELIAEIAAMIEMGAKLEDIGS 449 Query: 464 AVHAHPTLSEVLDELFKAAK 405 VH HPTLSE + E + A+ Sbjct: 450 TVHTHPTLSEAIMEAAQNAR 469
>DLDH_HALVO (Q04829) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide| dehydrogenase) Length = 474 Score = 60.5 bits (145), Expect = 4e-09 Identities = 27/74 (36%), Positives = 47/74 (63%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 F+A+ +AL N DG +++ ++G +LG I+G A++LI E + AI +G L+++ Sbjct: 386 FRASGRALTTNHADGFVRVVADEESGFVLGAQIVGPEASELIAELAFAIEMGATLEDVAS 445 Query: 464 AVHAHPTLSEVLDE 423 +H HPTL+E + E Sbjct: 446 TIHTHPTLAEAVME 459
>DLDH_RALEU (P52992) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 474 Score = 59.7 bits (143), Expect = 8e-09 Identities = 31/74 (41%), Positives = 43/74 (58%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 F AN +AL DG KM+ T EILGVHI+ +A+DLI EA A+ +++ Sbjct: 389 FMANGRALGMGHADGFVKMLADAKTDEILGVHIVAANASDLIAEAVVAMEFKAASEDIGR 448 Query: 464 AVHAHPTLSEVLDE 423 H HP++SEV+ E Sbjct: 449 VCHPHPSMSEVMRE 462
>DLDH_CHLMU (Q9PJI3) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 465 Score = 59.7 bits (143), Expect = 8e-09 Identities = 34/81 (41%), Positives = 47/81 (58%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K F+A KA+A E DG A +I + +ILG +++G HA+ LI E + AI Sbjct: 368 VKVTKFPFRAIGKAVAMGESDGFAAIISHETSQQILGAYVIGPHASSLISEITLAIRNEL 427 Query: 485 RLQELKLAVHAHPTLSEVLDE 423 L + +HAHPTL+EV E Sbjct: 428 TLPCIYETIHAHPTLAEVWAE 448
>DLDH_TRYCR (P90597) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide| dehydrogenase) Length = 477 Score = 58.9 bits (141), Expect = 1e-08 Identities = 33/79 (41%), Positives = 45/79 (56%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A A + DG K++ T ILGVHI+ A +LI EA A+ G Sbjct: 387 VGKFPFNANSRAKAVSTEDGFVKVLVDKATDRILGVHIVCTTAGELIGEACLAMEYGASS 446 Query: 479 QELKLAVHAHPTLSEVLDE 423 +++ HAHPT+SE L E Sbjct: 447 EDVGRTCHAHPTMSEALKE 465
>DLDH_MYCPN (P75393) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) Length = 457 Score = 58.5 bits (140), Expect = 2e-08 Identities = 27/74 (36%), Positives = 49/74 (66%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 KA+A+NE +G KM++ P TG+ILG I+ A+D+I E + A+ G + ++ ++ H Sbjct: 378 KAIADNETNGFVKMMFDPQTGKILGCCIIAATASDMIAELALAMGAGLTVFDIANSISPH 437 Query: 449 PTLSEVLDELFKAA 408 PT++E++ ++ K A Sbjct: 438 PTINEMIADVCKKA 451
>DLDH_CHLTE (Q8KCW2) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 469 Score = 58.2 bits (139), Expect = 2e-08 Identities = 32/81 (39%), Positives = 47/81 (58%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V+V ++ F A+ KA A + +G K+++ TG++LG H++G A +LI E A G Sbjct: 379 VAVGRSQFAASGKANAYGQLEGFVKLVFDAATGKMLGGHLIGHDAVELIGELGLACRYGV 438 Query: 485 RLQELKLAVHAHPTLSEVLDE 423 L VHAHPTLSE + E Sbjct: 439 TAGGLVNTVHAHPTLSETVRE 459
>DLDH3_PSEPU (P31046) Dihydrolipoyl dehydrogenase 3 (EC 1.8.1.4) (LPD-3)| (Dihydrolipoamide dehydrogenase 3) Length = 466 Score = 57.8 bits (138), Expect = 3e-08 Identities = 29/77 (37%), Positives = 45/77 (58%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A +E +G AK+I +T E+LGVH++G +++I E A+ Sbjct: 376 VGKFPFTANSRAKINHETEGFAKVIADAETDEVLGVHLVGPSVSEMIGEFCVAMEFSASA 435 Query: 479 QELKLAVHAHPTLSEVL 429 +++ L H HPT SE L Sbjct: 436 EDIALTCHPHPTRSEAL 452
>DLDH_MYCTU (P66004) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| alpha keto acid dehydrogenase complexes) (Dihydrolipoamide dehydrogenase) Length = 464 Score = 57.4 bits (137), Expect = 4e-08 Identities = 35/97 (36%), Positives = 46/97 (47%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K F AN KA + G K++ GE+LG H++G A+L+ E + A Sbjct: 372 VVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDL 431 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAKVNSGVSHSVN 375 EL VH HPT+SE L E F V H +N Sbjct: 432 TASELARNVHTHPTMSEALQECFHGL-----VGHMIN 463
>DLDH_MYCBO (P66005) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| alpha keto acid dehydrogenase complexes) (Dihydrolipoamide dehydrogenase) Length = 464 Score = 57.4 bits (137), Expect = 4e-08 Identities = 35/97 (36%), Positives = 46/97 (47%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K F AN KA + G K++ GE+LG H++G A+L+ E + A Sbjct: 372 VVVAKFPFTANAKAHGVGDPSGFVKLVADAKHGELLGGHLVGHDVAELLPELTLAQRWDL 431 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAKVNSGVSHSVN 375 EL VH HPT+SE L E F V H +N Sbjct: 432 TASELARNVHTHPTMSEALQECFHGL-----VGHMIN 463
>DLDH_CHLPN (Q9Z773) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 461 Score = 57.0 bits (136), Expect = 5e-08 Identities = 34/79 (43%), Positives = 45/79 (56%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 + K FKA KA+A DG A ++ T +ILG +++G HA+ LI E + AI L Sbjct: 367 LTKFPFKAIGKAVALGASDGFAAIVSHEITQQILGAYVIGPHASSLIGEMTLAIRNELTL 426 Query: 479 QELKLAVHAHPTLSEVLDE 423 + VHAHPTLSEV E Sbjct: 427 PCIYETVHAHPTLSEVWAE 445
>DLDH_BUCAP (Q8K9T7) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 476 Score = 56.6 bits (135), Expect = 6e-08 Identities = 27/70 (38%), Positives = 46/70 (65%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 + A+ +A A N G+ K+I+ +T +I+G I+G +A++LI E AI +G+ +++ L Sbjct: 382 WSASGRAHASNCTLGMTKLIFNKNTNKIIGGSIIGTNASELISEIGLAIEMGSDAEDISL 441 Query: 464 AVHAHPTLSE 435 +H HPTLSE Sbjct: 442 TIHPHPTLSE 451
>DLDH_ZYMMO (P50970) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 466 Score = 56.6 bits (135), Expect = 6e-08 Identities = 30/86 (34%), Positives = 45/86 (52%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + F AN KA+A+ DG K ++ D+G +LG H++G ++I + A L T Sbjct: 374 VKIGNFPFIANGKAIAQGATDGFVKTVFDADSGALLGAHMVGAEVTEMIQGYTVARTLET 433 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 E+ + HPTLSE + E AA Sbjct: 434 TEAEIMETIFPHPTLSEAMHESVLAA 459
>DLDH_MYCLE (Q50068) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| alpha keto acid dehydrogenase complexes) (Dihydrolipoamide dehydrogenase) Length = 467 Score = 56.6 bits (135), Expect = 6e-08 Identities = 34/97 (35%), Positives = 47/97 (48%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K F AN KA + G K++ GE+LG H++G + ++L+ E + A Sbjct: 375 VVVAKFPFTANAKAHGMGDPSGFVKLVADAKYGELLGGHMIGHNVSELLPELTLAQKWDL 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAKVNSGVSHSVN 375 EL VH HPTLSE L E F + H +N Sbjct: 435 TATELVRNVHTHPTLSEALQECFHGL-----IGHMIN 466
>DLDH_HAEIN (P43784) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 477 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/75 (36%), Positives = 45/75 (60%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K + A+ +A+A +G+ K+I+ DT +LG I+G + +L+ E AI +G Sbjct: 375 VAKFPWAASGRAIASECSEGMTKLIFDKDTHRVLGGAIVGSNGGELLGEIGLAIEMGCDA 434 Query: 479 QELKLAVHAHPTLSE 435 +++ L +HAHPTL E Sbjct: 435 EDIALTIHAHPTLHE 449
>DLDH_STAAW (P0A0E7) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_STAAU (P0A0E8) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_STAAS (Q6GAB8) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_STAAR (Q6GHY9) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_STAAN (P99084) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_STAAM (P0A0E6) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_STAAC (Q5HGY8) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) (Membrane-bound ribosome protein complex 50 kDa subunit) Length = 468 Score = 56.2 bits (134), Expect = 8e-08 Identities = 27/86 (31%), Positives = 48/86 (55%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + K + AN +AL+ ++ +G K+I + ++G ++G A+D+I E AI G Sbjct: 375 IKASKFPYAANGRALSLDDTNGFVKLITLKEDDTLIGAQVVGTGASDIISELGLAIEAGM 434 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAA 408 +++ L +HAHPTL E+ E + A Sbjct: 435 NAEDIALTIHAHPTLGEMTMEAAEKA 460
>DLDH_MANSE (O18480) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide| dehydrogenase) (E3) Length = 497 Score = 56.2 bits (134), Expect = 8e-08 Identities = 33/84 (39%), Positives = 44/84 (52%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A E DG K++ T ILG HI+G +LI+EA A G Sbjct: 406 VRKFPFLANSRAKTNGEPDGFVKVLSDKATDVILGTHIIGPGGGELINEAVLAQEYGAAA 465 Query: 479 QELKLAVHAHPTLSEVLDELFKAA 408 +++ HAHPT +E L E AA Sbjct: 466 EDVARVCHAHPTCAEALREANLAA 489
>DLDH_HALSA (Q9HN74) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide| dehydrogenase) Length = 474 Score = 55.8 bits (133), Expect = 1e-07 Identities = 26/74 (35%), Positives = 43/74 (58%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 F A+ +AL DG +++ ++G +LG I+G A++L+ E AI +G L+++ Sbjct: 386 FNASGRALTTGHDDGFVEVVADEESGFLLGAQIVGPEASELVAELGLAIEMGATLEDVAS 445 Query: 464 AVHAHPTLSEVLDE 423 +H HPTLSE E Sbjct: 446 TIHTHPTLSEATME 459
>DLDH_BUCAI (P57303) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 473 Score = 55.5 bits (132), Expect = 1e-07 Identities = 27/70 (38%), Positives = 43/70 (61%) Frame = -1 Query: 644 FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKL 465 + A+ +A+A N G K+I+ +I+G I+G +A +LI E AI +G +++ L Sbjct: 381 WNASGRAIASNCSIGKTKLIFNKQNNKIIGGSIVGSNAGELIGEVGLAIEMGCDAEDIAL 440 Query: 464 AVHAHPTLSE 435 +HAHPTLSE Sbjct: 441 TIHAHPTLSE 450
>DLDH_VIBPA (O50286) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 475 Score = 53.9 bits (128), Expect = 4e-07 Identities = 24/68 (35%), Positives = 43/68 (63%) Frame = -1 Query: 638 ANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAV 459 A+ +A+A + DG+ K+I+ +T ++G I+G + +L+ E AI +G +++ L + Sbjct: 383 ASGRAIASDCSDGMTKLIFDKETHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTI 442 Query: 458 HAHPTLSE 435 HAHPTL E Sbjct: 443 HAHPTLHE 450
>DLDH_VIBCH (Q9KPF6) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| 2-oxoglutarate dehydrogenase complex) (Dihydrolipoamide dehydrogenase) Length = 475 Score = 53.9 bits (128), Expect = 4e-07 Identities = 24/68 (35%), Positives = 43/68 (63%) Frame = -1 Query: 638 ANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAV 459 A+ +A+A + DG+ K+I+ +T ++G I+G + +L+ E AI +G +++ L + Sbjct: 383 ASGRAIASDCADGMTKLIFDKETHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTI 442 Query: 458 HAHPTLSE 435 HAHPTL E Sbjct: 443 HAHPTLHE 450
>DLDH_BUCBP (Q89AQ8) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) Length = 475 Score = 53.5 bits (127), Expect = 5e-07 Identities = 25/68 (36%), Positives = 44/68 (64%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +A++ +G+ K+I+ T +I+G I+G +A +L+ E S AI +G ++L L +HAH Sbjct: 388 RAVSSQCSEGVTKLIFDKKTNKIIGGCIVGSNAGELLGEISLAIEMGCDAEDLALTIHAH 447 Query: 449 PTLSEVLD 426 PTL E ++ Sbjct: 448 PTLYESIN 455
>DLDH3_BACSU (O34324) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| acetoin cleaving system) (Dihydrolipoamide dehydrogenase) Length = 458 Score = 53.1 bits (126), Expect = 7e-07 Identities = 32/82 (39%), Positives = 50/82 (60%), Gaps = 1/82 (1%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + + SF AN KAL + + +G K++ P+ GEI+GV ++G +LI +A+ AI G Sbjct: 366 VKIGEFSFSANGKALIKQQAEGKVKIMAEPEFGEIVGVSMIGPDVTELIGQAA-AIMNGE 424 Query: 485 RLQEL-KLAVHAHPTLSEVLDE 423 ++ + + AHPTLSE L E Sbjct: 425 MTADMAEHFIAAHPTLSETLHE 446
>DLDH_TRYBB (Q04933) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (Dihydrolipoamide| dehydrogenase) Length = 479 Score = 52.8 bits (125), Expect = 9e-07 Identities = 31/79 (39%), Positives = 43/79 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K F AN++A A DG K++ T ILGVHI+ A +LI A A+ G Sbjct: 389 VGKFPFNANSRAKAVATEDGFVKVLTDKATDRILGVHIVCSAAGELIAGALLAMEYGASS 448 Query: 479 QELKLAVHAHPTLSEVLDE 423 +++ HAHPT+SE + E Sbjct: 449 EDVGRTCHAHPTMSEAVKE 467
>DLDH_SHIFL (P0A9P3) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) Length = 473 Score = 52.4 bits (124), Expect = 1e-06 Identities = 23/68 (33%), Positives = 43/68 (63%) Frame = -1 Query: 638 ANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAV 459 A+ +A+A + DG+ K+I+ ++ ++G I+G + +L+ E AI +G +++ L + Sbjct: 382 ASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTI 441 Query: 458 HAHPTLSE 435 HAHPTL E Sbjct: 442 HAHPTLHE 449
>DLDH_ECOLI (P0A9P0) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) Length = 473 Score = 52.4 bits (124), Expect = 1e-06 Identities = 23/68 (33%), Positives = 43/68 (63%) Frame = -1 Query: 638 ANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAV 459 A+ +A+A + DG+ K+I+ ++ ++G I+G + +L+ E AI +G +++ L + Sbjct: 382 ASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTI 441 Query: 458 HAHPTLSE 435 HAHPTL E Sbjct: 442 HAHPTLHE 449
>DLDH_ECOL6 (P0A9P1) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) Length = 473 Score = 52.4 bits (124), Expect = 1e-06 Identities = 23/68 (33%), Positives = 43/68 (63%) Frame = -1 Query: 638 ANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAV 459 A+ +A+A + DG+ K+I+ ++ ++G I+G + +L+ E AI +G +++ L + Sbjct: 382 ASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTI 441 Query: 458 HAHPTLSE 435 HAHPTL E Sbjct: 442 HAHPTLHE 449
>DLDH_ECO57 (P0A9P2) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate and 2-oxoglutarate dehydrogenases complexes) (Dihydrolipoamide dehydrogenase) (Glycine cleavage system L protein) Length = 473 Score = 52.4 bits (124), Expect = 1e-06 Identities = 23/68 (33%), Positives = 43/68 (63%) Frame = -1 Query: 638 ANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAV 459 A+ +A+A + DG+ K+I+ ++ ++G I+G + +L+ E AI +G +++ L + Sbjct: 382 ASGRAIASDCADGMTKLIFDKESHRVIGGAIVGTNGGELLGEIGLAIEMGCDAEDIALTI 441 Query: 458 HAHPTLSE 435 HAHPTL E Sbjct: 442 HAHPTLHE 449
>DLDH_MYCGE (P47513) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| pyruvate complex) (Dihydrolipoamide dehydrogenase) Length = 457 Score = 51.2 bits (121), Expect = 3e-06 Identities = 28/88 (31%), Positives = 53/88 (60%), Gaps = 2/88 (2%) Frame = -1 Query: 665 VSVVKTS--FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIAL 492 + VK+S F + KA+A++E +G KM++ P TG ILG I+ A+D+I E + + Sbjct: 364 IDYVKSSLPFIYSGKAIADHETNGFVKMMFNPKTGAILGGCIIASTASDIIAELALVMEN 423 Query: 491 GTRLQELKLAVHAHPTLSEVLDELFKAA 408 + ++ ++ HPT++E++ ++ K A Sbjct: 424 NLTVFDIANSISPHPTMNEMVTDVCKKA 451
>DLDH1_PSEAE (Q9I1L9) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide dehydrogenase) (LPD-Val) Length = 464 Score = 48.5 bits (114), Expect = 2e-05 Identities = 22/79 (27%), Positives = 42/79 (53%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V F AN +A+ +G +++ R D ++G +G ++L + ++ +G RL Sbjct: 374 VASFPFAANGRAMTLEANEGFVRVVARRDNHLVVGWQAVGKAVSELSTAFAQSLEMGARL 433 Query: 479 QELKLAVHAHPTLSEVLDE 423 +++ +HAHPTL E + E Sbjct: 434 EDIAGTIHAHPTLGEAVQE 452
>DLDH1_PSEPU (P09063) Dihydrolipoyl dehydrogenase (EC 1.8.1.4) (E3 component of| branched-chain alpha-keto acid dehydrogenase complex) (Dihydrolipoamide dehydrogenase) (LPD-Val) Length = 459 Score = 47.4 bits (111), Expect = 4e-05 Identities = 23/79 (29%), Positives = 43/79 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V + F AN +A++ G +++ R D ILG +G+ ++L + ++ +G L Sbjct: 369 VAQFPFAANGRAMSLESKSGFVRVVARRDNHLILGWQAVGVAVSELSTAFAQSLEMGACL 428 Query: 479 QELKLAVHAHPTLSEVLDE 423 +++ +HAHPTL E + E Sbjct: 429 EDVAGTIHAHPTLGEAVQE 447
>STHA_PSEAE (P57112) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 463 Score = 43.5 bits (101), Expect = 6e-04 Identities = 26/78 (33%), Positives = 41/78 (52%), Gaps = 3/78 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K FK +A NE G+ K+++ +T EILGVH G A++++H + L Sbjct: 372 VGKAFFKGMARAQISNEPVGMLKILFHRETLEILGVHCFGDQASEIVHIGQAIMNQPGEL 431 Query: 479 QELKLAVHA---HPTLSE 435 LK V+ +PT++E Sbjct: 432 NTLKYFVNTTFNYPTMAE 449
>MERA_STRLI (P30341) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 474 Score = 43.1 bits (100), Expect = 7e-04 Identities = 22/67 (32%), Positives = 36/67 (53%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +AL + G+ K+I TG++L H+L A D+I A+ AI G + +L H + Sbjct: 389 RALVNRDTRGLVKLIAERGTGKLLAAHVLAEGAGDVITAATYAITAGLTVDQLARTWHPY 448 Query: 449 PTLSEVL 429 T++E L Sbjct: 449 LTMAEAL 455
>STHA_PSEPK (Q88KY8) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 463 Score = 41.6 bits (96), Expect = 0.002 Identities = 24/78 (30%), Positives = 40/78 (51%), Gaps = 3/78 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K FK+ +A E G+ K+++ +T EILGVH G A++++H + Sbjct: 372 VGKAFFKSMARAQIAGEPQGMLKILFHRETLEILGVHCFGYQASEIVHIGQAIMNQPGEQ 431 Query: 479 QELKLAVHA---HPTLSE 435 LK V+ +PT++E Sbjct: 432 NNLKYFVNTTFNYPTMAE 449
>STHA_PSEFL (O05139) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 463 Score = 40.8 bits (94), Expect = 0.004 Identities = 23/78 (29%), Positives = 40/78 (51%), Gaps = 3/78 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K FK+ +A E G+ K+++ +T E+LGVH G A++++H + Sbjct: 372 VGKAFFKSMARAQIAGEPQGMLKILFHRETLEVLGVHCFGYQASEIVHIGQAIMNQPGEQ 431 Query: 479 QELKLAVHA---HPTLSE 435 LK V+ +PT++E Sbjct: 432 NTLKYFVNTTFNYPTMAE 449
>MERA_BACCE (P16171) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 631 Score = 40.8 bits (94), Expect = 0.004 Identities = 24/79 (30%), Positives = 44/79 (55%), Gaps = 3/79 (3%) Frame = -1 Query: 656 VKTS---FKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 VKTS A +AL E G+ K++ T ++LG H++ +A D+I+ A+ A+ G Sbjct: 534 VKTSVLPLDAVPRALVNRETTGVFKLVADAKTLKVLGAHVVAENAGDVIYAATLAVKFGL 593 Query: 485 RLQELKLAVHAHPTLSEVL 429 + +L+ + + T++E L Sbjct: 594 TVGDLRETMAPYLTMAEGL 612
>TYTR_LEIDO (P39050) Trypanothione reductase (EC 1.8.1.12) (TR)| (N(1),N(8)-bis(glutathionyl)spermidine reductase) Length = 491 Score = 40.0 bits (92), Expect = 0.006 Identities = 17/55 (30%), Positives = 30/55 (54%) Frame = -1 Query: 593 KMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVL 429 ++I GE+LGVH+LG A ++I + +G ++ + + HPT +E L Sbjct: 414 RIITNESNGEVLGVHMLGDSAPEIIQSVGICMKMGAKISDFHSTIGVHPTSAEEL 468
>GSHR_BURCE (P48639) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 449 Score = 39.3 bits (90), Expect = 0.011 Identities = 19/77 (24%), Positives = 37/77 (48%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + ++F+ AL+ + + K++ ++G HI+G AA++I + AI Sbjct: 364 VEIYGSAFRPMRAALSGRDEKALVKLVVNGSNDRVVGAHIVGADAAEIIQGIAVAIKARA 423 Query: 485 RLQELKLAVHAHPTLSE 435 + + HPTL+E Sbjct: 424 TKADFDATLGVHPTLAE 440
>GSHR_ANASP (P48638) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 459 Score = 39.3 bits (90), Expect = 0.011 Identities = 18/77 (23%), Positives = 41/77 (53%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V++ +T F+ + + + K++ T ++LG H++G +AA++I + A+ +G Sbjct: 377 VTIYRTRFRPMYHSFTGKQERIMMKLVVDTKTDKVLGAHMVGENAAEIIQGVAIAVKMGA 436 Query: 485 RLQELKLAVHAHPTLSE 435 ++ V HP+ +E Sbjct: 437 TKKDFDATVGIHPSSAE 453
>TYTR_TRYCR (P28593) Trypanothione reductase (EC 1.8.1.12) (TR)| (N(1),N(8)-bis(glutathionyl)spermidine reductase) Length = 492 Score = 39.3 bits (90), Expect = 0.011 Identities = 18/57 (31%), Positives = 31/57 (54%) Frame = -1 Query: 599 IAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVL 429 +AK+I G +LGVH+LG +A ++I + L ++ + + HPT +E L Sbjct: 412 VAKIITNHSDGTVLGVHLLGDNAPEIIQGVGICLKLNAKISDFYNTIGVHPTSAEEL 468
>STHA_PSESM (Q884I6) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 463 Score = 39.3 bits (90), Expect = 0.011 Identities = 22/78 (28%), Positives = 40/78 (51%), Gaps = 3/78 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K FK +A E G+ K+++ +T E+LGVH G A++++H ++ Sbjct: 372 VGKAFFKGMARAQISGERVGMLKILFHRETLEVLGVHCFGDQASEIVHIGQAIMSQPGEA 431 Query: 479 QELKLAVHA---HPTLSE 435 +K V+ +PT++E Sbjct: 432 NTIKYFVNTTFNYPTMAE 449
>STHA_AZOVI (Q9XBQ9) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 464 Score = 38.9 bits (89), Expect = 0.014 Identities = 23/78 (29%), Positives = 39/78 (50%), Gaps = 3/78 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V K FK +A E G+ K+++ +T EILGVH G A++++H + Sbjct: 373 VGKAFFKGMARAQIAVEKAGMLKILFHRETLEILGVHCFGYQASEIVHIGQAIMNQKGEA 432 Query: 479 QELKLAVHA---HPTLSE 435 LK ++ +PT++E Sbjct: 433 NTLKYFINTTFNYPTMAE 450
>YMER_STAAU (P08655) Hypothetical 19.7 kDa protein in mercuric resistance| operon Length = 180 Score = 38.1 bits (87), Expect = 0.024 Identities = 19/57 (33%), Positives = 31/57 (54%) Frame = -1 Query: 614 NEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPT 444 NE K++ D +I+G H++ A +LI+ + AI G +ELK + A+PT Sbjct: 115 NEDFAAFKVLIDEDHDQIVGAHLISNEADELINHFATAIRFGISTKELKQMIFAYPT 171
>STHA_VIBCH (P50529) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 466 Score = 38.1 bits (87), Expect = 0.024 Identities = 25/90 (27%), Positives = 44/90 (48%), Gaps = 3/90 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRL 480 V + SFK +A + G K+++ +T EILG+H G AA++IH + Sbjct: 375 VGRASFKHLARAQIAGKDIGSLKILFHRETKEILGIHCFGERAAEIIHIGQAIMEQKGEA 434 Query: 479 QELKLAVHA---HPTLSEVLDELFKAAKVN 399 ++ V+ +PT++E F+ A +N Sbjct: 435 NTIEYFVNTTFNYPTMAEA----FRVAALN 460
>YKGC_ECOLI (P77212) Probable pyridine nucleotide-disulfide oxidoreductase ykgC| Length = 441 Score = 38.1 bits (87), Expect = 0.024 Identities = 23/87 (26%), Positives = 41/87 (47%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + VV A +A N+ G+ K I T +LG +L + + ++I+ + G Sbjct: 355 IQVVTLPVAAIPRARVMNDTRGVLKAIVDNKTQRMLGASLLCVDSHEMINIVKMVMDAGL 414 Query: 485 RLQELKLAVHAHPTLSEVLDELFKAAK 405 L+ + HP++SE L++LF K Sbjct: 415 PYSILRDQIFTHPSMSESLNDLFSLVK 441
>TYTR_TRYBB (P39051) Trypanothione reductase (EC 1.8.1.12) (TR)| (N(1),N(8)-bis(glutathionyl)spermidine reductase) Length = 492 Score = 38.1 bits (87), Expect = 0.024 Identities = 17/57 (29%), Positives = 30/57 (52%) Frame = -1 Query: 599 IAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVL 429 +AK++ G +LGVH+LG A ++I + L ++ + + HPT +E L Sbjct: 412 VAKIVTNHSDGTVLGVHLLGDGAPEIIQAVGVCLRLNAKISDFYNTIGVHPTSAEEL 468
>TYTR_CRIFA (P39040) Trypanothione reductase (EC 1.8.1.12) (TR)| (N(1),N(8)-bis(glutathionyl)spermidine reductase) Length = 491 Score = 38.1 bits (87), Expect = 0.024 Identities = 24/83 (28%), Positives = 42/83 (50%), Gaps = 4/83 (4%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDT----GEILGVHILGLHAADLIHEASNAI 498 V+V ++SF T + G K + R T GE+LGVH+LG + ++I + + Sbjct: 389 VAVYESSF---TPLMHNISGSTYKKFMVRIVTNHADGEVLGVHMLGDSSPEIIQSVAICL 445 Query: 497 ALGTRLQELKLAVHAHPTLSEVL 429 +G ++ + + HPT +E L Sbjct: 446 KMGAKISDFYNTIGVHPTSAEEL 468
>GSHR_STRTR (Q60151) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 450 Score = 38.1 bits (87), Expect = 0.024 Identities = 23/77 (29%), Positives = 37/77 (48%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + V K+SF AL +N K++ + +I+G+H +G ++I S AI +G Sbjct: 368 IKVYKSSFTPMYTALGDNRQLSTMKLVTLGEDEKIIGLHGIGYGVDEMIQGFSVAIKMGA 427 Query: 485 RLQELKLAVHAHPTLSE 435 + V HPT SE Sbjct: 428 TKADFDNTVAIHPTGSE 444
>MERA_SHEPU (Q54465) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 557 Score = 37.7 bits (86), Expect = 0.031 Identities = 23/66 (34%), Positives = 34/66 (51%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA E DG K++ TG ++G IL +LI A A+A+ R+ +LA Sbjct: 472 RALANFETDGFIKLVTEKATGRLIGAQILAHEGGELIQSA--ALAIRNRMTVTELADQLF 529 Query: 449 PTLSEV 432 P L+ V Sbjct: 530 PYLTMV 535
>STHA_VIBVY (Q7MQ83) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 466 Score = 37.7 bits (86), Expect = 0.031 Identities = 18/48 (37%), Positives = 29/48 (60%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V ++SFK +A + G K+++ +T EILG+H G AA++IH Sbjct: 375 VGRSSFKHLARAQIAGKDIGSLKILFHRETKEILGIHCFGERAAEIIH 422
>STHA_VIBVU (Q8DD46) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 466 Score = 37.7 bits (86), Expect = 0.031 Identities = 18/48 (37%), Positives = 29/48 (60%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V ++SFK +A + G K+++ +T EILG+H G AA++IH Sbjct: 375 VGRSSFKHLARAQIAGKDIGSLKILFHRETKEILGIHCFGERAAEIIH 422
>STHA_VIBPA (Q87KN5) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 466 Score = 37.7 bits (86), Expect = 0.031 Identities = 18/48 (37%), Positives = 29/48 (60%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V ++SFK +A + G K+++ +T EILG+H G AA++IH Sbjct: 375 VGRSSFKHLARAQIAGKDVGSLKILFHRETKEILGIHCFGERAAEIIH 422
>STHA_MYCTU (P66006) Probable soluble pyridine nucleotide transhydrogenase (EC| 1.6.1.1) (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 468 Score = 37.7 bits (86), Expect = 0.031 Identities = 18/56 (32%), Positives = 31/56 (55%) Frame = -1 Query: 602 GIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSE 435 G+ K++ + ++LGVHI G A +++H + G ++ L AV +PT SE Sbjct: 392 GMLKLLVSTEDLKLLGVHIFGTSATEMVHIGQAVMGCGGSVEYLVDAVFNYPTFSE 447
>STHA_MYCBO (P66007) Probable soluble pyridine nucleotide transhydrogenase (EC| 1.6.1.1) (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 468 Score = 37.7 bits (86), Expect = 0.031 Identities = 18/56 (32%), Positives = 31/56 (55%) Frame = -1 Query: 602 GIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSE 435 G+ K++ + ++LGVHI G A +++H + G ++ L AV +PT SE Sbjct: 392 GMLKLLVSTEDLKLLGVHIFGTSATEMVHIGQAVMGCGGSVEYLVDAVFNYPTFSE 447
>GSHR_YARLI (Q6C5H4) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 470 Score = 37.0 bits (84), Expect = 0.053 Identities = 21/79 (26%), Positives = 38/79 (48%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V + F A A+ E + K++ +++G+HI+G +A+++ AI +G Sbjct: 388 VKVYTSKFVAMYYAMLEEKAPTAYKLVCAGKDEKVVGLHIVGADSAEILQGFGVAIRMGA 447 Query: 485 RLQELKLAVHAHPTLSEVL 429 + V HPT +E L Sbjct: 448 TKADFDNVVAIHPTSAEEL 466
>GSHR_ASHGO (Q74ZK4) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 480 Score = 37.0 bits (84), Expect = 0.053 Identities = 20/77 (25%), Positives = 39/77 (50%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + + +T F A A+ E++ K+I +++G+HI+G +A+++ AI +G Sbjct: 398 IKIYQTKFTAMYYAMLEDKSPTKYKLICAGPEEKVVGLHIVGDGSAEILQGFGVAIKMGA 457 Query: 485 RLQELKLAVHAHPTLSE 435 + V HPT +E Sbjct: 458 TKADFDSCVAIHPTSAE 474
>GSHR_HUMAN (P00390) Glutathione reductase, mitochondrial precursor (EC| 1.8.1.7) (GR) (GRase) Length = 522 Score = 36.6 bits (83), Expect = 0.070 Identities = 20/79 (25%), Positives = 37/79 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V TSF A+ + + + KM+ +++G+H+ GL +++ + A+ +G Sbjct: 440 VKTYSTSFTPMYHAVTKRKTKCVMKMVCANKEEKVVGIHMQGLGCDEMLQGFAVAVKMGA 499 Query: 485 RLQELKLAVHAHPTLSEVL 429 + V HPT SE L Sbjct: 500 TKADFDNTVAIHPTSSEEL 518
>GSHR_CANGA (Q6FRV2) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 476 Score = 36.2 bits (82), Expect = 0.091 Identities = 21/79 (26%), Positives = 39/79 (49%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + V + F A A+ E++ K+I +++G+HI+G +A+++ AI +G Sbjct: 394 IKVYTSKFTAMYYAMLEHKSPTRYKIICEGPNEKVVGLHIVGDSSAEILQGFGVAIKMGA 453 Query: 485 RLQELKLAVHAHPTLSEVL 429 + V HPT +E L Sbjct: 454 TKADFDNCVAIHPTSAEEL 472
>GSHR_CAEEL (P30635) Probable glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 503 Score = 35.4 bits (80), Expect = 0.15 Identities = 20/80 (25%), Positives = 41/80 (51%), Gaps = 3/80 (3%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDG---IAKMIYRPDTGEILGVHILGLHAADLIHEASNAIA 495 + V + F + +N+ G + + R ++ +ILG+H +G +AA++I + A Sbjct: 402 IEVFHSHFTPFEYVVPQNKDSGFCYVKAVCTRDESQKILGLHFVGPNAAEVIQGYAVAFR 461 Query: 494 LGTRLQELKLAVHAHPTLSE 435 +G + +L+ + HP SE Sbjct: 462 VGISMSDLQNTIAIHPCSSE 481
>GSHR_PSEAE (P23189) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 451 Score = 35.4 bits (80), Expect = 0.15 Identities = 16/77 (20%), Positives = 36/77 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + ++ F+ L +++ + K++ +LG H++G A +++ + A+ G Sbjct: 365 VKIFESRFRPMKLTLTDDQEKTLMKLVVDAHDDRVLGCHMVGAEAGEILQGIAVAMKAGA 424 Query: 485 RLQELKLAVHAHPTLSE 435 Q + HPT +E Sbjct: 425 TKQAFDETIGIHPTAAE 441
>TYTR_TRYCO (P13110) Trypanothione reductase (EC 1.8.1.12) (TR)| (N(1),N(8)-bis(glutathionyl)spermidine reductase) Length = 492 Score = 35.0 bits (79), Expect = 0.20 Identities = 16/57 (28%), Positives = 30/57 (52%) Frame = -1 Query: 599 IAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVL 429 +AK+I G ++GVH+LG + ++I + L ++ + + HPT +E L Sbjct: 412 VAKIITDHGDGTVVGVHLLGDSSPEIIQAVGICMKLNAKISDFYNTIGVHPTSAEEL 468
>STHA_SHIFL (Q83MI1) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 466 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 375 VGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIH 422
>GSHR_NEUCR (Q873E8) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 468 Score = 35.0 bits (79), Expect = 0.20 Identities = 21/81 (25%), Positives = 41/81 (50%), Gaps = 2/81 (2%) Frame = -1 Query: 665 VSVVKTSFKANTKALA--ENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIAL 492 + + K+SF A A+ E++ K+I +++G+HI+GL + +++ A+ + Sbjct: 384 LKIYKSSFTAMYYAMMKPEDKAPTAYKLICAGPEEKVVGLHIIGLGSGEILQGFGVAVNM 443 Query: 491 GTRLQELKLAVHAHPTLSEVL 429 G + V HPT +E L Sbjct: 444 GATKADFDNCVAIHPTSAEEL 464
>GSHR_DEBHA (Q6BPI1) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 490 Score = 35.0 bits (79), Expect = 0.20 Identities = 20/82 (24%), Positives = 42/82 (51%), Gaps = 3/82 (3%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEG---DGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIA 495 + + K+ F A A+ E++ K++ + +++G+HI+G +A+++ AI Sbjct: 405 IKIYKSKFNAMYYAMMEDDSLKSPTSYKVVCAGEDEKVVGLHIVGDSSAEILQGFGVAIK 464 Query: 494 LGTRLQELKLAVHAHPTLSEVL 429 +G ++ V HPT +E L Sbjct: 465 MGATKKDFDSCVAIHPTSAEEL 486
>STHA_SALTY (P66008) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 465 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 374 VGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIH 421
>STHA_SALTI (P66009) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 465 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 374 VGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIH 421
>STHA_PHOLL (Q7MBG9) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 465 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 374 VGRAQFKHLARAQIAGMNVGSLKILFHRETKEILGIHCFGERAAEIIH 421
>STHA_ECOLI (P27306) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 465 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 374 VGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIH 421
>STHA_ECOL6 (Q8FB93) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 465 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 374 VGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIH 421
>STHA_ECO57 (Q8X727) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 465 Score = 35.0 bits (79), Expect = 0.20 Identities = 17/48 (35%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T EILG+H G AA++IH Sbjct: 374 VGRAQFKHLARAQIVGMNVGTLKILFHRETKEILGIHCFGERAAEIIH 421
>GSHR_MOUSE (P47791) Glutathione reductase, mitochondrial precursor (EC| 1.8.1.7) (GR) (GRase) Length = 500 Score = 35.0 bits (79), Expect = 0.20 Identities = 18/79 (22%), Positives = 37/79 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + T+F A+ + + KM+ +++G+H+ G+ +++ + A+ +G Sbjct: 418 VKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGA 477 Query: 485 RLQELKLAVHAHPTLSEVL 429 + V HPT SE L Sbjct: 478 TKADFDNTVAIHPTSSEEL 496
>GSHR_RAT (P70619) Glutathione reductase (EC 1.8.1.7) (GR) (GRase) (Fragment)| Length = 424 Score = 34.7 bits (78), Expect = 0.26 Identities = 18/79 (22%), Positives = 37/79 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + T+F A+ + + KM+ +++G+H+ G+ +++ + A+ +G Sbjct: 342 VKIYSTAFTPMYHAVTTRKTKCVMKMVCANKEEKVVGIHMQGIGCDEMLQGFAVAVKMGA 401 Query: 485 RLQELKLAVHAHPTLSEVL 429 + V HPT SE L Sbjct: 402 TKADFDNRVAIHPTSSEEL 420
>STHA_YERPE (Q8ZA97) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) Length = 466 Score = 34.3 bits (77), Expect = 0.35 Identities = 21/78 (26%), Positives = 36/78 (46%), Gaps = 3/78 (3%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAI---ALG 489 V + FK +A G K+++ +T +ILG+H G AA++IH + G Sbjct: 375 VGRAQFKHLARAQIVGMDTGSLKILFHRETKQILGIHCFGERAAEIIHIGQAIMEQKGEG 434 Query: 488 TRLQELKLAVHAHPTLSE 435 L+ +PT++E Sbjct: 435 NTLEYFVNTTFNYPTMAE 452
>TRXR2_BOVIN (Q9N2I8) Thioredoxin reductase 2, mitochondrial precursor (EC| 1.8.1.9) (TR3) Length = 511 Score = 34.3 bits (77), Expect = 0.35 Identities = 17/48 (35%), Positives = 27/48 (56%) Frame = -1 Query: 563 ILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 +LG+H LG +A ++I + I G Q+L V HPT +E + +L Sbjct: 447 VLGLHFLGPNAGEVIQGFALGIKCGASYQQLMRTVGIHPTCAEEVAKL 494
>GSHRP_ARATH (P42770) Glutathione reductase, chloroplast precursor (EC 1.8.1.7)| (GR) (GRase) Length = 565 Score = 33.9 bits (76), Expect = 0.45 Identities = 20/77 (25%), Positives = 35/77 (45%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V ++F+ L+ K+I +T ++LGVH+ G + ++I A+ G Sbjct: 458 VDVYTSNFRPLKATLSGLPDRVFMKLIVCANTNKVLGVHMCGEDSPEIIQGFGVAVKAGL 517 Query: 485 RLQELKLAVHAHPTLSE 435 + V HPT +E Sbjct: 518 TKADFDATVGVHPTAAE 534
>GSHR_YEAST (P41921) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 483 Score = 33.5 bits (75), Expect = 0.59 Identities = 19/79 (24%), Positives = 37/79 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + V + F A A+ + K++ +++G+HI+G +A+++ AI +G Sbjct: 401 IKVYNSKFTAMYYAMLSEKSPTRYKIVCAGPNEKVVGLHIVGDSSAEILQGFGVAIKMGA 460 Query: 485 RLQELKLAVHAHPTLSEVL 429 + V HPT +E L Sbjct: 461 TKADFDNCVAIHPTSAEEL 479
>GSHR_KLULA (Q6HA23) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 484 Score = 33.5 bits (75), Expect = 0.59 Identities = 21/81 (25%), Positives = 39/81 (48%), Gaps = 2/81 (2%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIA--KMIYRPDTGEILGVHILGLHAADLIHEASNAIAL 492 V V + F A A+ E + K++ + +++G+HI+G +A+++ AI + Sbjct: 400 VKVYNSKFNAMYYAMMEEKDKTPTRYKLVCTGEEEKVVGLHIIGDSSAEILQGFGVAIKM 459 Query: 491 GTRLQELKLAVHAHPTLSEVL 429 G + V HPT +E L Sbjct: 460 GATKADFDSCVAIHPTSAEEL 480
>STHA_PECCC (P71317) Soluble pyridine nucleotide transhydrogenase (EC 1.6.1.1)| (STH) (NAD(P)(+) transhydrogenase [B-specific]) (Fragment) Length = 150 Score = 33.5 bits (75), Expect = 0.59 Identities = 16/48 (33%), Positives = 26/48 (54%) Frame = -1 Query: 659 VVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIH 516 V + FK +A G K+++ +T +ILG+H G AA++IH Sbjct: 59 VGRAQFKHLARAQIVGMNVGSLKILFHRETKQILGIHCFGERAAEIIH 106
>GSHR_HAEIN (P43783) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 456 Score = 33.5 bits (75), Expect = 0.59 Identities = 21/77 (27%), Positives = 37/77 (48%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K+SF A A+ ++ K++ +++G+H +G ++I + AI +G Sbjct: 374 VKVYKSSFTAMYTAVTQHRQPCKMKLVCVGKDEKVVGLHGIGFGVDEMIQGFAVAIKMGA 433 Query: 485 RLQELKLAVHAHPTLSE 435 + V HPT SE Sbjct: 434 TKADFDNTVAIHPTGSE 450
>GSHRP_SPIOL (Q43154) Glutathione reductase, chloroplast precursor (EC 1.8.1.7)| (GR) (GRase) (Fragment) Length = 489 Score = 33.1 bits (74), Expect = 0.77 Identities = 17/77 (22%), Positives = 36/77 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + V +SF ++ + I K++ +T ++LG + G AA+++ + A+ G Sbjct: 391 ILVFTSSFNPMKNTISGRQEKTIMKLVVDAETDKVLGASMCGPDAAEIMQGIAIALKFGA 450 Query: 485 RLQELKLAVHAHPTLSE 435 + V HP+ +E Sbjct: 451 TKAQFDSTVGIHPSAAE 467
>MERA_SERMA (P08662) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| (Fragments) Length = 460 Score = 32.7 bits (73), Expect = 1.0 Identities = 20/67 (29%), Positives = 34/67 (50%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA + G K++ +G ++GV ++ A +LI A AI +QEL + + Sbjct: 375 RALANFDTRGFIKLVIEEGSGRLIGVQVVAPEAGELIQTAVLAIRNRMTVQELADQLFPY 434 Query: 449 PTLSEVL 429 T+ E L Sbjct: 435 LTMVEGL 441
>GSHR_ECOLI (P06715) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 450 Score = 32.7 bits (73), Expect = 1.0 Identities = 19/77 (24%), Positives = 37/77 (48%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V K+SF A A+ + K++ +I+G+H +G +++ + A+ +G Sbjct: 368 VKVYKSSFTAMYTAVTTHRQPCRMKLVCVGSEEKIVGIHGIGFGMDEMLQGFAVALKMGA 427 Query: 485 RLQELKLAVHAHPTLSE 435 ++ V HPT +E Sbjct: 428 TKKDFDNTVAIHPTAAE 444
>GSHRP_PEA (P27456) Glutathione reductase, chloroplast/mitochondrial precursor| (EC 1.8.1.7) (GR) (GRase) (GOR1) Length = 552 Score = 32.3 bits (72), Expect = 1.3 Identities = 19/77 (24%), Positives = 33/77 (42%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 + V +F+ L+ K+I +T +LG+H+ G AA++ + I G Sbjct: 444 IDVFTANFRPMKATLSGLPDRVFMKLIVSAETNVVLGLHMCGEDAAEIAQGFAVGIKAGL 503 Query: 485 RLQELKLAVHAHPTLSE 435 + V HPT +E Sbjct: 504 TKADFDATVGIHPTAAE 520
>TRXR1_PONPY (Q5NVA2) Thioredoxin reductase 1, cytoplasmic (EC 1.8.1.9) (TR)| (TR1) Length = 499 Score = 32.3 bits (72), Expect = 1.3 Identities = 15/62 (24%), Positives = 30/62 (48%) Frame = -1 Query: 575 DTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDELFKAAKVNS 396 D ++G H+LG +A ++ + A+ G ++L + HP +EV L A + + Sbjct: 431 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTLSVAKRSGA 490 Query: 395 GV 390 + Sbjct: 491 SI 492
>MERA_SHIFL (P08332) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 564 Score = 32.3 bits (72), Expect = 1.3 Identities = 20/67 (29%), Positives = 34/67 (50%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA + G K++ +G ++GV + A +LI A+ AI +QEL + + Sbjct: 479 RALANFDTRGFIKLVVEEGSGRLIGVQAVAPEAGELIQTAALAIRNRMTVQELADQLFPY 538 Query: 449 PTLSEVL 429 T+ E L Sbjct: 539 LTMVEGL 545
>MERA_THIFE (P17239) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 547 Score = 32.3 bits (72), Expect = 1.3 Identities = 20/67 (29%), Positives = 34/67 (50%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA G K++ +G ++GV ++ A +LI A+ AI +QEL + + Sbjct: 462 RALANFNTRGFIKLVAEVGSGRLIGVQVVAPEAGELIQTAALAIRNRMTVQELADQLFPY 521 Query: 449 PTLSEVL 429 T+ E L Sbjct: 522 LTMVEGL 528
>GSHR_SCHPO (P78965) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 464 Score = 32.3 bits (72), Expect = 1.3 Identities = 19/81 (23%), Positives = 37/81 (45%), Gaps = 2/81 (2%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGD--GIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIAL 492 + V T F ++ E E K++ +++G+H++G +A+++ AI + Sbjct: 380 IKVYNTKFNGLNYSMVEQEDKVPTTYKLVCAGPLQKVVGLHLVGDFSAEILQGFGVAIKM 439 Query: 491 GTRLQELKLAVHAHPTLSEVL 429 G + V HPT +E L Sbjct: 440 GATKSDFDSCVAIHPTSAEEL 460
>GSHRC_ORYSA (P48642) Glutathione reductase, cytosolic (EC 1.8.1.7) (GR) (GRase)| Length = 496 Score = 32.3 bits (72), Expect = 1.3 Identities = 17/77 (22%), Positives = 36/77 (46%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V V +SF ++++ + + K++ +T ++LG + G A ++I + A+ G Sbjct: 398 VLVYTSSFNPMKNSISKRQEKTVMKLVVDSETDKVLGASMCGPDAPEIIQGMAVALKCGA 457 Query: 485 RLQELKLAVHAHPTLSE 435 V HP+ +E Sbjct: 458 TKATFDSTVGIHPSAAE 474
>TRXR1_MOUSE (Q9JMH6) Thioredoxin reductase 1, cytoplasmic (EC 1.8.1.9) (TR)| (TR1) Length = 499 Score = 32.0 bits (71), Expect = 1.7 Identities = 14/52 (26%), Positives = 26/52 (50%) Frame = -1 Query: 575 DTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 D ++G H+LG +A ++ + A+ G Q+L + HP +E+ L Sbjct: 431 DDERVVGFHVLGPNAGEVTQGFAAALKCGLTKQQLDSTIGIHPVCAEIFTTL 482
>TRXR2_DROME (Q9VNT5) Thioredoxin reductase 2, mitochondrial precursor (EC| 1.8.1.9) (TrxR-2) Length = 516 Score = 31.6 bits (70), Expect = 2.2 Identities = 22/70 (31%), Positives = 33/70 (47%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 KA+AE GD +ILG+H +G A ++I + A+ G ++ L V H Sbjct: 441 KAVAEVSGDQ-----------KILGLHYIGPVAGEVIQGFAAALKTGLTVKTLLNTVGIH 489 Query: 449 PTLSEVLDEL 420 PT +E L Sbjct: 490 PTTAEEFTRL 499
>TRXR1_PIG (Q9MYY8) Thioredoxin reductase 1, cytoplasmic (EC 1.8.1.9) (TR)| (TR1) Length = 499 Score = 31.2 bits (69), Expect = 2.9 Identities = 14/52 (26%), Positives = 26/52 (50%) Frame = -1 Query: 575 DTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 D ++G H+LG +A ++ + A+ G ++L + HP +EV L Sbjct: 431 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
>TRXR1_HUMAN (Q16881) Thioredoxin reductase 1, cytoplasmic precursor (EC| 1.8.1.9) (TR) (TR1) Length = 499 Score = 31.2 bits (69), Expect = 2.9 Identities = 14/52 (26%), Positives = 26/52 (50%) Frame = -1 Query: 575 DTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 D ++G H+LG +A ++ + A+ G ++L + HP +EV L Sbjct: 431 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKKQLDSTIGIHPVCAEVFTTL 482
>GSHRP_TOBAC (P80461) Glutathione reductase, chloroplast precursor (EC 1.8.1.7)| (GR) (GRase) (Fragment) Length = 557 Score = 31.2 bits (69), Expect = 2.9 Identities = 15/53 (28%), Positives = 27/53 (50%) Frame = -1 Query: 593 KMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSE 435 K+I T ++LG+H+ G A +++ + A+ G + V HPT +E Sbjct: 474 KLIVCAKTSKVLGLHMCGDDAPEIVQGFAIAVKAGLTKADFDATVGIHPTSAE 526
>MERA_ALCSP (P94188) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 559 Score = 31.2 bits (69), Expect = 2.9 Identities = 20/67 (29%), Positives = 33/67 (49%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA + G K++ +G ++GV + A +LI A AI +QEL + + Sbjct: 474 RALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPY 533 Query: 449 PTLSEVL 429 T+ E L Sbjct: 534 LTMVEGL 540
>MERA_PSEFL (Q51772) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 548 Score = 31.2 bits (69), Expect = 2.9 Identities = 20/67 (29%), Positives = 33/67 (49%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA + G K++ +G ++GV + A +LI A AI +QEL + + Sbjct: 463 RALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPY 522 Query: 449 PTLSEVL 429 T+ E L Sbjct: 523 LTMVEGL 529
>MERA_ENTAG (P94702) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 561 Score = 31.2 bits (69), Expect = 2.9 Identities = 20/67 (29%), Positives = 33/67 (49%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA + G K++ +G ++GV + A +LI A AI +QEL + + Sbjct: 476 RALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPY 535 Query: 449 PTLSEVL 429 T+ E L Sbjct: 536 LTMVEGL 542
>MERA_ACICA (Q52109) Mercuric reductase (EC 1.16.1.1) (Hg(II) reductase)| Length = 561 Score = 31.2 bits (69), Expect = 2.9 Identities = 20/67 (29%), Positives = 33/67 (49%) Frame = -1 Query: 629 KALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAH 450 +ALA + G K++ +G ++GV + A +LI A AI +QEL + + Sbjct: 476 RALANFDTRGFIKLVIEEGSGRLIGVQAVAPEAGELIQTAVLAIRNRMTVQELADQLFPY 535 Query: 449 PTLSEVL 429 T+ E L Sbjct: 536 LTMVEGL 542
>TRXR1_BOVIN (O62768) Thioredoxin reductase 1, cytoplasmic (EC 1.8.1.9) (TR)| (TR1) Length = 499 Score = 30.8 bits (68), Expect = 3.8 Identities = 14/52 (26%), Positives = 25/52 (48%) Frame = -1 Query: 575 DTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 D ++G H+LG +A ++ + A+ G +L + HP +EV L Sbjct: 431 DNERVVGFHVLGPNAGEVTQGFAAALKCGLTKDQLDSTIGIHPVCAEVFTTL 482
>THSA_SULTO (O24734) Thermosome subunit alpha (Thermosome subunit 1)| (Chaperonin alpha subunit) Length = 559 Score = 30.8 bits (68), Expect = 3.8 Identities = 26/83 (31%), Positives = 39/83 (46%) Frame = -1 Query: 557 GVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDELFKAAKVNSGVSHSV 378 GV ++ AD + + + + Q LK AV A + ++ D+L AA + SG Sbjct: 484 GVDVMNGKIADDMLALNVLEPVRVKAQVLKSAVEAATAILKI-DDLIAAAPLKSG----- 537 Query: 377 NEPVAA*RRAGTRAKSSTPASLE 309 E + G KSSTP+SLE Sbjct: 538 -EKKGEKKEGGEEEKSSTPSSLE 559
>TRXR_PLAF7 (P61076) Thioredoxin reductase (EC 1.8.1.9) (TrxR)| Length = 541 Score = 30.8 bits (68), Expect = 3.8 Identities = 17/74 (22%), Positives = 40/74 (54%), Gaps = 1/74 (1%) Frame = -1 Query: 599 IAKMI-YRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDE 423 +AK++ + + ++G H +G +A ++ + A+ L + ++ + HPT +E Sbjct: 459 LAKLVCLKNEDNRVIGFHYVGPNAGEVTQGMALALRLKVKKKDFDNCIGIHPTDAESFMN 518 Query: 422 LFKAAKVNSGVSHS 381 LF ++SG+S++ Sbjct: 519 LF--VTISSGLSYA 530
>TRXR_PLAF5 (Q25861) Thioredoxin reductase (EC 1.8.1.9) (TrxR)| Length = 541 Score = 30.8 bits (68), Expect = 3.8 Identities = 17/74 (22%), Positives = 40/74 (54%), Gaps = 1/74 (1%) Frame = -1 Query: 599 IAKMI-YRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDE 423 +AK++ + + ++G H +G +A ++ + A+ L + ++ + HPT +E Sbjct: 459 LAKLVCLKNEDNRVIGFHYVGPNAGEVTQGMALALRLKVKKKDFDNCIGIHPTDAESFMN 518 Query: 422 LFKAAKVNSGVSHS 381 LF ++SG+S++ Sbjct: 519 LF--VTISSGLSYA 530
>GSHRC_PEA (Q43621) Glutathione reductase, cytosolic (EC 1.8.1.7) (GR) (GRase)| (GOR2) Length = 498 Score = 30.4 bits (67), Expect = 5.0 Identities = 19/98 (19%), Positives = 41/98 (41%), Gaps = 1/98 (1%) Frame = -1 Query: 665 VSVVKTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGT 486 V + ++F ++ + + K++ T ++LG + G A +++ + AI G Sbjct: 400 VLIFTSTFNPMKNTISGRQEKTVMKLVVDAQTDKVLGASMCGPDAPEIVQGIAIAIKCGA 459 Query: 485 RLQELKLAVHAHPTLSEVLDEL-FKAAKVNSGVSHSVN 375 + V HP+ +E + + +V GV N Sbjct: 460 TKAQFDSTVGIHPSSAEEFVTMRSETRRVTGGVKPKTN 497
>ILVB_KLETE (Q04524) Acetolactate synthase, catabolic (EC 2.2.1.6) (ALS)| Length = 559 Score = 30.0 bits (66), Expect = 6.5 Identities = 22/86 (25%), Positives = 40/86 (46%) Frame = -1 Query: 626 ALAENEGDGIAKMIYRPDTGEILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHP 447 A A +EGD + LG + A L+H++ + +A+ + + + + V A Sbjct: 93 ATANSEGDPVVA----------LGGAVKRADKAKLVHQSMDTVAMFSPVTKYAVEVTASD 142 Query: 446 TLSEVLDELFKAAKVNSGVSHSVNEP 369 L+EV+ F+AA+ S V+ P Sbjct: 143 ALAEVVSNAFRAAEQGRPGSAFVSLP 168
>GSHR_PLAFK (Q94655) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 499 Score = 29.6 bits (65), Expect = 8.5 Identities = 12/43 (27%), Positives = 25/43 (58%) Frame = -1 Query: 563 ILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSE 435 I G+HI+GL+A +++ + A+ + ++ + HPT +E Sbjct: 447 IKGLHIIGLNADEIVQGFAVALKMNATKKDFDETIPIHPTAAE 489
>GSHR_PLAF7 (O15770) Glutathione reductase (EC 1.8.1.7) (GR) (GRase)| Length = 499 Score = 29.6 bits (65), Expect = 8.5 Identities = 12/43 (27%), Positives = 25/43 (58%) Frame = -1 Query: 563 ILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSE 435 I G+HI+GL+A +++ + A+ + ++ + HPT +E Sbjct: 447 IKGLHIIGLNADEIVQGFAVALKMNATKKDFDETIPIHPTAAE 489
>GLMM_CORGL (Q8NST4) Phosphoglucosamine mutase (EC 5.4.2.10)| Length = 447 Score = 29.6 bits (65), Expect = 8.5 Identities = 24/80 (30%), Positives = 31/80 (38%) Frame = -1 Query: 470 KLAVHAHPTLSEVLDELFKAAKVNSGVSHSVNEPVAA*RRAGTRAKSSTPASLEGP*FHY 291 KL H + V+D L GV + E A R K + P SLEG Sbjct: 122 KLPDHVEDEIERVMDSLPAEGPTGHGVGRVIEEATDAQDRYLEHLKEAVPTSLEGIKIVV 181 Query: 290 EPAVFPATRSAPLA*QGAFA 231 + A A+ AP A + A A Sbjct: 182 DAANGAASVVAPTAYEAAGA 201
>TRXR2_RAT (Q9Z0J5) Thioredoxin reductase 2, mitochondrial precursor (EC| 1.8.1.9) (TR3) Length = 526 Score = 29.6 bits (65), Expect = 8.5 Identities = 15/48 (31%), Positives = 25/48 (52%) Frame = -1 Query: 563 ILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 +LG+H LG +A ++ + I G ++ V HPT SE + +L Sbjct: 462 VLGLHFLGPNAGEVTQGFALGIQCGASYAQVMQTVGIHPTCSEEVVKL 509
>TRXR2_MOUSE (Q9JLT4) Thioredoxin reductase 2, mitochondrial precursor (EC| 1.8.1.9) (TR3) Length = 524 Score = 29.6 bits (65), Expect = 8.5 Identities = 15/48 (31%), Positives = 25/48 (52%) Frame = -1 Query: 563 ILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 +LG+H LG +A ++ + I G ++ V HPT SE + +L Sbjct: 460 VLGLHFLGPNAGEVTQGFALGIKCGASYAQVMQTVGIHPTCSEEVVKL 507
>TRXR2_HUMAN (Q9NNW7) Thioredoxin reductase 2, mitochondrial precursor (EC| 1.8.1.9) (TR3) (TR-beta) (Selenoprotein Z) (SelZ) Length = 524 Score = 29.6 bits (65), Expect = 8.5 Identities = 15/48 (31%), Positives = 25/48 (52%) Frame = -1 Query: 563 ILGVHILGLHAADLIHEASNAIALGTRLQELKLAVHAHPTLSEVLDEL 420 +LG+H LG +A ++ + I G ++ V HPT SE + +L Sbjct: 460 VLGLHFLGPNAGEVTQGFALGIKCGASYAQVMRTVGIHPTCSEEVVKL 507
>LEC1_CLALU (Q39528) Agglutinin-1 precursor (Agglutinin I) (ClAI) (LecClAI)| [Contains: Agglutinin-1 subunit A; Agglutinin-1 subunit B] Length = 293 Score = 29.6 bits (65), Expect = 8.5 Identities = 18/62 (29%), Positives = 33/62 (53%), Gaps = 1/62 (1%) Frame = -1 Query: 653 KTSFKANTKALAENEGDGIAKMIYRPDTGEILGVHILGL-HAADLIHEASNAIALGTRLQ 477 KT+F + ++ GDG A I PDT G +LGL + +L + ++N +A+ + Sbjct: 106 KTTFSFAITSPTQDPGDGFAFFIAPPDTTPGYGGGLLGLFNGFNLRNSSNNGVAVNNQSA 165 Query: 476 EL 471 ++ Sbjct: 166 QI 167 Database: uniprot_sprot.fasta Posted date: May 25, 2006 5:36 PM Number of letters in database: 80,573,946 Number of sequences in database: 219,361 Lambda K H 0.318 0.135 0.401 Gapped Lambda K H 0.267 0.0410 0.140 Matrix: BLOSUM62 Gap Penalties: Existence: 11, Extension: 1 Number of Hits to DB: 90,067,757 Number of Sequences: 219361 Number of extensions: 1851651 Number of successful extensions: 4836 Number of sequences better than 10.0: 136 Number of HSP's better than 10.0 without gapping: 4680 Number of HSP's successfully gapped in prelim test: 0 Number of HSP's that attempted gapping in prelim test: 0 Number of HSP's gapped (non-prelim): 4833 length of database: 80,573,946 effective HSP length: 108 effective length of database: 56,882,958 effective search space used: 6427774254 frameshift window, decay const: 50, 0.1 T: 12 A: 40 X1: 16 ( 7.3 bits) X2: 38 (14.6 bits) X3: 64 (24.7 bits) S1: 41 (21.7 bits)
