>H281DRAFT_01517 FitnessBrowser__Burk376:H281DRAFT_01517
MLAAVLHEPKLIRIDEVAPPEPGPGQVRVRVRAGGICGSDLSYYFKGKSGDFAVREPFVLGHEVAGEIDSLGEGVSADARLVPGQRVAVNPGLACGTCKYCTIGMPNHCLNMRFMGSASTFPHTQGMFRQYIVVAARQCIPVADSVDFAQASMAEPLAVALHAVKRAGSLVGASVLLIGCGPIGCILLSVARRAGAHRVVAVDLSSRALQVAAQLGADQTVNAADSATIEQWSAQRGTFDVVIEASGSPAGLETALRSARAGGTVIQVGNLPAGQSPVAANLVMSKELRYQGSFRFTDEYAIAADEIASGKVDLRPLMTHAFAMSDANQAFEVALDRSQSMKVHLNFD
>biolip__6dkhC The crystal structure of l-idonate 5-dehydrogenase from escherichia coli str. K-12 substr. Mg1655
SNAMQVKTQSCVVAGKKTVAVTEQTIDWNNNGTLVQITRGGICGSDLHYYQEGKVGNFMIKAPMVLGHEVIGKVIHSDSSELHEGQTVAINPSKPCGHCKYCIEHNENQCTDMRFFGSAMYFPHVDGGFTRYKMVETSQCVPYPAKADEKVMAFAEPLAVAIHAAHQAGELQGKRVFISGVGPIGCLIVSAVKTLGAAEIVCADVSPRSLSLGKEMGADVLVNPQNDDMDHWKAEKGYFDVSFEVSGHPSSVNTCLEVTRARGVMVQVGMGGAMAEFPMMTLIGKEISLRGSFRFTSEFNTAVSWLANGVINPLPLLSAEYPFTDLEEALRFAGDKTQAAKVQLVF
>ecocyc__IDONDEHYD-MONOMER L-idonate 5-dehydrogenase (EC 1.1.1.264) (Escherichia coli K-12 substr. MG1655)
MQVKTQSCVVAGKKTVAVTEQTIDWNNNGTLVQITRGGICGSDLHYYQEGKVGNFMIKAPMVLGHEVIGKVIHSDSSELHEGQTVAINPSKPCGHCKYCIEHNENQCTDMRFFGSAMYFPHVDGGFTRYKMVETSQCVPYPAKADEKVMAFAEPLAVAIHAAHQAGELQGKRVFISGVGPIGCLIVSAVKTLGAAEIVCADVSPRSLSLGKEMGADVLVNPQNDDMDHWKAEKGYFDVSFEVSGHPSSVNTCLEVTRARGVMVQVGMGGAMAEFPMMTLIGKEISLRGSFRFTSEFNTAVSWLANGVINPLPLLSAEYPFTDLEEALRFAGDKTQAAKVQLVF
>SwissProt__P0DMQ6 Sorbitol dehydrogenase; SDH; Polyol dehydrogenase; EC 1.1.1.- (Gallus gallus (Chicken))
MAATGQNLAVVVHRAGDLRLENRPIPEPGPNEVLLRMHSVGICGSDVHYWQHGRIGDFVVKDPMVLGHEASGTVIKVGAGVTHLKPGDRVAIEPGVPRETDEFCKTGRYNLSPTIFFCATPPDDGNLCRYYKHSASYCYKLPDSVTFEEGALIEPLSVGIHACKRAGVTLGSRVFVSGSGPIGLVNVIIAKMMGAAAVVVTDLSASRLQTAKELGADFTIQIKNETPQEVAAKVESLLGCMPEITVECTGVQACIQASIYATRSGGTLVLVGLGPEMVTVPIVNAAVREVDIRGIFRYCNTWPVAISLLASKRINIKPLVTHRFPLEKALEAFETTKRGEGVKIMLKCDPTDQNP
>metacyc__MONOMER-11719 D-sorbitol dehydrogenase (EC 1.1.1.14) (Malus domestica)
MGKGGMSDGDHADRCCGEAINGDVQQENMAAWLLGVKNLKIQPYKLPNLGPHDVRVRLRAVGICGSDVHHFKNMRCVDFIVKEPMVIGHECAGIIEEVGSEVEHLVPGDRVALEPGISCKRCNLCKQGRYNLCRKMKFFGSPPNNGCLANQVVHPGDLCFKLPDNVSLEEGAMCEPLSVGIHACRRANVCQETNVLVVGAGPIGLVTLLAARAFGAPRIVIADVNDERLLIAKSLGADAVVKVSTNIEDVAEEVAKIQKVLENGVDVTFDCAGFNKTITTALSATRPGGKVCLVGMGQREMTLPLATREIDVIGIFRYQNTWPLCLEFLRSGKIDVKPLITHRFGFSQKEVEEAFETSARGGNAIKVMFNL
>BRENDA__Q5I6M4 L-iditol 2-dehydrogenase (EC 1.1.1.14) (Malus domestica)
MGKGGMSDGDHADRCCGEAINGDVQQENMAAWLLGVKNLKIQPYKLPNLGPHDVRVRLKAVGICGSDVHHFKNMRCVDFIVKEPMVIGHECAGIIEEVGSEVEDLVPGDRVALEPGISCKRCNLCKQGRYNLCRKMKFFGSPPNNGCLANQVVHPGDLCFKLPDNVSLEEGAMCEPLSVGIHACRRANVCQETNVLVVGAGPIGLVTLLAARAFGAPRIVIADVNDERLLIAKSLGADAVVKVSTNIEDVAEEVAKIQKVLENGVDVTFDCAGFNKTITTALSATRPGGKVCLVGMGQREMTLPLATREIDVIGIFRYQNTWPLCLEFLRSGKIDVKPLITHRFGFSQKEVEEAFETSARGGNAIKVMFNL
>metacyc__MONOMER-16192 L-idonate 5-dehydrogenase (EC 1.1.1.366) (Vitis vinifera)
MGKGGNSEDAVSGKEHGEENMAAWLLGIKTLKIQPYILPSLGPYDVKVRIKAVGICGSDVHHFKTMRCANFIVKKPMVIGHECAGIIEEVGSEVKNLVAGDRVALEPGISCNRCSLCRNGQYNLCREMKFFGSPPTNGSLANQVVHPSNLCFKLPDNVSLEEGAMCEPLSVGIHACRRANVGPETNVLIMGSGPIGLVTMLAARAFGAPRIVLVDVDDQRLAIAKDLGADDIIRVSTNIQDLDEEVAKIQSTMVTGVDVSFDCVGFNKTMSTALNATRAGGKVCLVGLAQSEMTVPLTPAAAREVDIVGIFRYRNTWPLCLEFLRSGKIDVKPLITHRFTFSQKDVEEAFETSARGGNAIKVMFNL
>BRENDA__Q5I6M3 L-iditol 2-dehydrogenase (EC 1.1.1.14) (Malus domestica)
MGKGGQSCNGMVRQAKPVEQENMAAWLVDVNTIKILPFKLPSIGPNDVRIRIKAVGICGSDVHYLKTMKCADFEVKEPMVIGHECAGIVDKVGSEVKHLVPGDRVAVEPGISCARCQQCKGGRYNLCPDMKFFATPPVHGSLANQIVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRANVGPETTVLIIGAGPIGLVSVLAARAFGAPRIVIVDMDDKRLAMAKSLGADEAVKVSTKMEDLDDEVAEIKEAMISEVDVTFDCVGFNKTMSTGLNATRPGGKVCLVGMGHGVMTVPLTPAAAREVDVVGVFRYQNTWPLCLEFLRSGKIDVKPLITHRFGFTEKEVEEAFATSARGGNAIKVMFKL
>BRENDA__Q3C2L6 L-iditol 2-dehydrogenase (EC 1.1.1.14) (Solanum lycopersicum)
MGKGGSDENMAAWLLGVNTLKIQPFNLPALGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGGEVKTLVPGDRVALEPGISCWRCNLCKEGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPDDISLEEGAMCEPLSVGVHACRRANVGPETNILVLGAGPIGLVTLLAARAFGAPRIVIVDVDDYRLSVAKKLGADDIVKVSINIQDVATDIENIQKAMGGGIDASFDCAGFNKTMSTALGATRPGGKVCLVGMGHHEMTVPLTPAAAREVDVIGIFRYKNTWPLCLEFLRSGKIDVKPLITHRFGFSQEEVEEAFETSARGGDAIKVMFNL
>SwissProt__Q9FJ95 Sorbitol dehydrogenase; SDH; Polyol dehydrogenase; Ribitol dehydrogenase; RDH; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.56; EC 1.1.1.9 (Arabidopsis thaliana (Mouse-ear cress))
MGKGGMSQGEGSKVEEENMAAWLVGINTLKIQPFLLPSVGPHDVRVRMKAVGICGSDVHYLKTMRCADFVVKEPMVIGHECAGIIEEVGEEVKHLVVGDRVALEPGISCWRCNLCREGRYNLCPEMKFFATPPVHGSLANQVVHPADLCFKLPENVSLEEGAMCEPLSVGVHACRRAEVGPETNVLVMGAGPIGLVTMLAARAFSVPRIVIVDVDENRLAVAKQLGADEIVQVTTNLEDVGSEVEQIQKAMGSNIDVTFDCAGFNKTMSTALAATRCGGKVCLVGMGHGIMTVPLTPAAAREVDVVGVFRYKNTWPLCLEFLTSGKIDVKPLITHRFGFSQKEVEDAFETSARGSNAIKVMFNL
>metacyc__BSU06150-MONOMER glucitol dehydrogenase monomer (EC 1.1.1.9; EC 1.1.1.14) (Bacillus subtilis (strain 168))
MTHTVPQNMKAAVMHNTREIKIETLPVPDINHDEVLIKVMAVGICGSDLHYYTNGRIGNYVVEKPFILGHECAGEIAAVGSSVDQFKVGDRVAVEPGVTCGRCEACKEGRYNLCPDVQFLATPPVDGAFVQYIKMRQDFVFLIPDSLSYEEAALIEPFSVGIHAAARTKLQPGSTIAIMGMGPVGLMAVAAAKAFGAGTIIVTDLEPLRLEAAKKMGATHIINIREQDALEEIKTITNDRGVDVAWETAGNPAALQSALASVRRGGKLAIVGLPSQNEIPLNVPFIADNEIDIYGIFRYANTYPKGIEFLASGIVDTKHLVTDQYSLEQTQDAMERALQFKNECLKVMVYPNR
>biolip__1pl6A Human sdh/nadh/inhibitor complex
AAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNFIVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFCATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCGAGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQLGCKPEVTIECTGAEASIQAGIYATRSGGTLVLVGLGSEMTTVPLLHAAIREVDIKGVFRYCNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
>SwissProt__Q00796 Sorbitol dehydrogenase; SDH; (R,R)-butanediol dehydrogenase; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Ribitol dehydrogenase; RDH; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.4; EC 1.1.1.14; EC 1.1.1.56; EC 1.1.1.9 (Homo sapiens (Human))
MAAAAKPNNLSLVVHGPGDLRLENYPIPEPGPNEVLLRMHSVGICGSDVHYWEYGRIGNFIVKKPMVLGHEASGTVEKVGSSVKHLKPGDRVAIEPGAPRENDEFCKMGRYNLSPSIFFCATPPDDGNLCRFYKHNAAFCYKLPDNVTFEEGALIEPLSVGIHACRRGGVTLGHKVLVCGAGPIGMVTLLVAKAMGAAQVVVTDLSATRLSKAKEIGADLVLQISKESPQEIARKVEGQLGCKPEVTIECTGAEASIQAGIYATRSGGNLVLVGLGSEMTTVPLLHAAIREVDIKGVFRYCNTWPVAISMLASKSVNVKPLVTHRFPLEKALEAFETFKKGLGLKIMLKCDPSDQNP
>biolip__1e3jA Ketose reductase (sorbitol dehydrogenase) from silverleaf whitefly
DNLSAVLYKQNDLRLEQRPIPEPKEDEVLLQMAYVGICGSDVHYYEHGRIADFIVKDPMVIGHEASGTVVKVGKNVKHLKKGDRVAVEPGVPCRRCQFCKEGKYNLCPDLTFCATPPDDGNLARYYVHAADFCHKLPDNVSLEEGALLEPLSVGVHACRRAGVQLGTTVLVIGAGPIGLVSVLAAKAYGAFVVCTARSPRRLEVAKNCGADVTLVVDPAKEEESSIIERIRSAIGDLPNVTIDCSGNEKCITIGINITRTGGTLMLVGMGSQMVTVPLVNACAREIDIKSVFRYCNDYPIALEMVASGRCNVKQLVTHSFKLEQTVDAFEAARKKADNTIKVMISCRQ
>SwissProt__Q58D31 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 (Bos taurus (Bovine))
MAAAKPENLSLVVHGPGDLRLENYPIPEPGPNEVLLKMHSVGICGSDVHYWQHGRIGDFVVKKPMVLGHEASGTVVKVGSLVRHLQPGDRVAIEPGAPRETDEFCKIGRYNLSPTIFFCATPPDDGNLCRFYKHNANFCYKLPDNVTFEEGALIEPLSVGIHACRRAGVTLGNKVLVCGAGPIGLVSLLAAKAMGAAQVVVTDLSASRLSKAKEVGADFILQISNESPQEIAKKVEGLLGSKPEVTIECTGVETSIQAGIYATHSGGTLVLVGLGSEMTSVPLVHAATREVDIKGVFRYCNTWPMAISMLASKSVNVKPLVTHRFPLEKALEAFETSKKGLGLKVMIKCDPNDQNP
>SwissProt__Q64442 Sorbitol dehydrogenase; SDH; SORD; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 (Mus musculus (Mouse))
MAAPAKGENLSLVVHGPGDIRLENYPIPELGPNDVLLKMHSVGICGSDVHYWEHGRIGDFVVKKPMVLGHEAAGTVTKVGELVKHLKPGDRVAIEPGVPREVDEYCKIGRYNLTPTIFFCATPPDDGNLCRFYKHNADFCYKLPDSVTFEEGALIEPLSVGIYACRRGSVSLGNKVLVCGAGPVGMVTLLVAKAMGAAQVVVTDLSASRLTKAKEVGADFTIQVGKETPQEIASKVESLLGSKPEVTIECTGAESSVQTGIYATHSGGTLVIVGMGAEMVNLPLVHAAIREVDIKGVFRYCNTWPMAISMLASKTLNVKPLVTHRFPLEKAVEAFETAKKGVGLKVMIKCDPNDQNP
>biolip__3qe3A Sheep liver sorbitol dehydrogenase
AENLSLVVHGPGDLRLENYPIPEPGPNEVLLKMHSVGICGSDVHYWQHGRIGDFVVKKPMVLGHEASGTVVKVGSLVRHLQPGDRVAIQPGAPRQTDEFCKIGRYNLSPTIFFCATPPDDGNLCRFYKHNANFCYKLPDNVTFEEGALIEPLSVGIHACRRAGVTLGNKVLVCGAGPIGLVNLLAAKAMGAAQVVVTDLSASRLSKAKEVGADFILEISNESPEEIAKKVEGLLGSKPEVTIECTGVETSIQAGIYATHSGGTLVLVGLGSEMTSVPLVHAATREVDIKGVFRYCNTWPMAISMLASKSVNVKPLVTHRFPLEKALEAFETSKKGLGLKVMIKCDPSDQNP
>SwissProt__P27867 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 (Rattus norvegicus (Rat))
MAAPAKGENLSLVVHGPGDIRLENYPIPELGPNDVLLKMHSVGICGSDVHYWEHGRIGDFVVKKPMVLGHEAAGTVTKVGPMVKHLKPGDRVAIEPGVPREIDEFCKIGRYNLTPSIFFCATPPDDGNLCRFYKHSADFCYKLPDSVTFEEGALIEPLSVGIYACRRGSVSLGNKVLVCGAGPIGIVTLLVAKAMGASQVVVIDLSASRLAKAKEVGADFTIQVAKETPHDIAKKVESVLGSKPEVTIECTGAESSVQTGIYATHSGGTLVVVGMGPEMINLPLVHAAVREVDIKGVFRYCNTWPMAVSMLASKTLNVKPLVTHRFPLEKAVEAFETAKKGLGLKVMIKCDPNDQNP
>SwissProt__P07846 Sorbitol dehydrogenase; SDH; L-iditol 2-dehydrogenase; Polyol dehydrogenase; Xylitol dehydrogenase; XDH; EC 1.1.1.-; EC 1.1.1.14; EC 1.1.1.9 (Ovis aries (Sheep))
AKPAAENLSLVVHGPGDLRLENYPIPEPGPNEVLLKMHSVGICGSDVHYWQGRIGDFVVKKPMVLGHEASGTVVKVGSLVRHLQPGDRVAIQPGAPRQTDEFCKIGRYNLSPTIFFCATPPDDGNLCRFYKHNANFCYKLPDNVTFEEGALIEPLSVGIHACRRAGVTLGNKVLVCGAGPIGLVNLLAAKAMGAAQVVVTDLSASRLSKAKEVGADFILEISNESPEEIAKKVEGLLGSKPEVTIECTGVETSIQAGIYATHSGGTLVLVGLGSEMTSVPLVHAATREVDIKGVFRYCNTWPMAISMLASKSVNVKPLVTHRFPLEKALEAFETSKKGLGLKVMIKCDPSDQNP
>metacyc__MONOMER-21872 D-xylulose reductase (EC 1.1.1.9) (Aspergillus niger)
MSTQNTNAQNLSFVLEGIHRVKFEDRPIPEINNPHDVLVNVRFTGICGSDVHYWEHGSIGQFIVKDPMVLGHESSGVVSKVGSAVTSLKVGDCVAMEPGIPCRRCEPCKAGKYNLCVKMAFAATPPYDGTLAKYYVLPEDFCYKLPESITLQEGAIMEPLSVAVHIVKQAGINPGQSVVVFGAGPVGLLCCAVAKAYGASKVIAVDIQKGRLDFAKKYAATATFEPAKAAALENAQRIITENDLGSGADVAIDASGAEPSVHTGIHVLRAGGTYVQGGMGRSEITFPIMAACTKELNVKGSFRYGSGDYKLAVSLVSAGKVNVKELITGVVKFEDAERAFEEVRAGKGIKTLIAGVDS
>BRENDA__Q2K0Q7 D-xylulose reductase (EC 1.1.1.9) (Rhizobium etli)
MTKVRALVLERQHELALRDIDLPLETGAGQVKIKIHTVGVCGSDVHYYTHGKIGPFVVNAPMVLGHEAAGTVVEVGSGVRHLKVGDRVCMEPGIPDPNSKASRLGMYNIDPAVSFWATPPVHGVLTPEVVHPANYTFKLPDNVSFAEGAMVEPFAVGMQAASKAKIAPGDTAIVLGAGPIGTMVAIAALAGGCARAIVADLAQPKLDIAAQYQGVIPVNIRETNLIEEVGQLTDGWGADVVFECSGSPKAWETIMALPRPGGVIVAVGLPVNPVGFDVSTATTKEIRIETVFRYAHQYERSIALLGSGRVDLKPLISETFKFEDSIKAFDRAAEARPSDVKLQIVME
>metacyc__MONOMER-13193 D-sorbitol dehydrogenase (EC 1.1.1.14; EC 1.1.1.9) (Hypocrea jecorina)
MATQTINKDAISNLSFVLNKPGDVTFEERPKPTITDPNDVLVAVNYTGICGSDVHYWVHGAIGHFVVKDPMVLGHESAGTVVEVGPAVKSLKPGDRVALEPGYPCRRCSFCRAGKYNLCPDMVFAATPPYHGTLTGLWAAPADFCYKLPDGVSLQEGALIEPLAVAVHIVKQARVQPGQSVVVMGAGPVGLLCAAVAKAYGASTIVSVDIVQSKLDFARGFCSTHTYVSQRISAEDNAKAIKELAGLPGGADVVIDASGAEPSIQTSIHVVRMGGTYVQGGMGKSDITFPIMAMCLKEVTVRGSFRYGAGDYELAVELVRTGRVDVKKLITGTVSFKQAEEAFQKVKSGEAIKILIAGPNEKV
>SwissProt__Q07993 D-xylulose reductase; Xylitol dehydrogenase; XDH; EC 1.1.1.9 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MTDLTTQEAIVLERPGKITLTNVSIPKISDPNEVIIQIKATGICGSDIHYYTHGRIANYVVESPMVLGHESSGIVALIGENVKTLKVGDRVALEPGIPDRFSPEMKEGRYNLDPNLKFAATPPFDGTLTKYYKTMKDFVYKLPDDVSFEEGALIEPLSVAIHANKLAKIKFGARCVVFGAGPIGLLAGKVASVFGAADVVFVDLLENKLETARQFGATHIVNSGDLPHGVTVDSVIKKAIGKKGADVVFECSGAEPCVRAGIEVCKAGGTIVQVGMGQEEIQFPISIIPTKELTFQGCFRYCQGDYSDSIELVSSRKLSLKPFITHRYSFKDAVEAFEETSHHPLNNIKTIIEGPE
>SwissProt__P36624 Sorbitol dehydrogenase; SDH; Polyol dehydrogenase; Protein tms1; EC 1.1.1.- (Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast))
MAPAEKAFVLRKKMDTAIEDRPGQTLTDDHQVKVAIKATGICGSDVHYWKEGGIGDFILKKPMILGHESAGVVVEVGKGVSSLKPGDPVAVEPGCVCRLCDYCRSGRYNLCPHMEFAATPPYDGTLRTYYITTEDFCTKLPKQISVEEGALFEPMSVAVHAMTRGNLKCGSRVLVMGCGTVGLLMMAVAKAYGAIDIVAVDASPSRVEFAQKYVGAKPFTPIAAKENESLPDYAQRYKQAIIEKYGEFDFAVDATGVGICIHTAVLALKRGGTFVQAGNGKPVIDFPINHIINYEINVLGSFRYAHGCYKQSLFLVSNGLVDVKPLITHRFAFKDALKAYETVASGEEGVLKVIIGGPDA
>BRENDA__A0A3S7PMC4 D-xylulose reductase (EC 1.1.1.9) (Torulaspora delbrueckii)
MASQEAVVLEKKELIQIESRPIPEIKNPHDVKIQIKATGICGSDVHYFTHGSIGDFVVKAPLVLGHESSGVVVEVGDAVSSVKVGDRVAVEPGVPSRYSKETMSGHYNLCPHMAFAATPPYDGTLVKYYLSPEDFVYKLADHISFEEGAVVEPLSVAVHANRLANTAFGQAALVLGAGPVGLLAGAVAKAFGATDVVFVDIFESKLEKAKQFGATHTVLFKPDSDENDLVSLVTKSLGGLHPDVVFECSGAEKCIRAAVKSVKRGGTFVQVGMGKDNINFPINEFSQKEATFKGCFRYYEGDFDDAVKLLSTGKVNVKPLITKVFPFEQAVEAYKHNVEHAKDVTKTIITGPQ
>metacyc__MONOMER-13192 NAD<sup>+</sup>-dependent xylitol dehydrogenase (EC 1.1.1.9) (Aspergillus oryzae (strain ATCC 42149 / RIB 40))
MGAPPKTAQNLSFVLEGIHKVKFEDRPIPQLRDAHDVLVDVRFTGICGSDVHYWEHGSIGQFVVKDPMVLGHESSGVISKVGSAVTTLKVGDHVAMEPGIPCRRCEPCKEGKYNLCEKMAFAATPPYDGTLAKYYVLPEDFCYKLPENINLQEAAVMEPLSVAVHIVKQANVAPGQSVVVFGAGPVGLLCCAVARAFGSPKVIAVDIQKGRLEFAKKYAATAIFEPSKVSALENAERIVNENDLGRGADIVIDASGAEPSVHTGIHVLRPGGTYVQGGMGRNEITFPIMAACTKELNVRGSFRYGSGDYKLAVNLVASGKVSVKELITGVVSFEDAEQAFHEVKAGKGIKTLIAGVDV
>BRENDA__S6BFC0 D-xylulose reductase (EC 1.1.1.9) (Rhizomucor pusillus)
MSPVSDPKKNNSFVLQKQDEISFEDRPVPVAGPGQVIVNIKATGICGSDVHYWTHGRIGHFVCNGPMVLGHESAGIVTSLGEGVIDLKVGDRVALEPGVPCGRCEMCKIGKYNLCPDMAFAATPPYDGTLCDYYRHSADFCYKLPDNVSLEEGALIEPLSVGIHAARRGEVRLGDRVFVFGAGPVGLLTAAAARAAGASHITMADISESRLKFAKSYIADETVHMTSKPPRDVDTNEFAKAEAEKLFQSGITPANVVFDCTGVEVCVQMSVYLVKNNGKIILVGMGASVQSISVADVSAREVDVRGVMRYCNTYPTAIEVLASEKVDLKSLITHRYKFEDSIKAFQHVKEGREGTIKVVITNE
>SwissProt__P35497 Sorbitol dehydrogenase 1; SDH 1; Polyol dehydrogenase; Xylitol dehydrogenase; EC 1.1.1.-; EC 1.1.1.9 (Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast))
MSQNSNPAVVLEKVGDIAIEQRPIPTIKDPHYVKLAIKATGICGSDIHYYRSGGIGKYILKAPMVLGHESSGQVVEVGDAVTRVKVGDRVAIEPGVPSRYSDETKEGRYNLCPHMAFAATPPIDGTLVKYYLSPEDFLVKLPEGVSYEEGACVEPLSVGVHSNKLAGVRFGTKVVVFGAGPVGLLTGAVARAFGATDVIFVDVFDNKLQRAKDFGATNTFNSSQFSTDKAQDLADGVQKLLGGNHADVVFECSGADVCIDAAVKTTKVGGTMVQVGMGKNYTNFPIAEVSGKEMKLIGCFRYSFGDYRDAVNLVATGKVNVKPLITHKFKFEDAAKAYDYNIAHGGEVVKTIIFGPE
>BRENDA__Q07786 L-iditol 2-dehydrogenase (EC 1.1.1.14) (Saccharomyces cerevisiae)
MSQNSNPAVVLEKVGDIAIEQRPIPTIKDPHYVKLAIKATGICGSDIHYYRSGGIGKYILKAPMVLGHESSGQVVEVGDAVTRVKVGDRVAIEPGVPSRYSDETKEGSYNLCPHMAFAATPPIDGTLVKYYLSPEDFLVKLPEGVSYEEGACVEPLSVGVHSNKLAGVRFGTKVVVFGAGPVGLLTGAVARAFGATDVIFVDVFDNKLQRAKDFGATNTFNSSQFSTDKAQDLADGVQKLLGGNHADVVFECSGADVCIDAAVKTTKVGGTMVQVGMGKNYTNFPIAEVSGKEMKLIGCFRYSFGDYRDAVNLVATGKVNVKPLITHKFKFEDAAKAYDYNIAHGGEVVKTIIFGPE
>metacyc__MONOMER-17164 L-arabinitol dehydrogenase (EC 1.1.1.12; EC 1.1.1.9; EC 1.1.1.14) (Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513))
MTSSVVRLGQKCPAFVLHPGGRFDYEERVIPNLQTDRDVIVQVIVTGLCGSDIHYWQHGRIGRYVVEAPIVLGHESAGIVVECGSKSGFAIGDRVALEPGIACNTCHHCRAGRYNLCSAMRFAATPPYDGTLATYYRLPAECCYKLPAHVSLQHGALVEPLSVAVHSCRLAGDMQQKSVVVFGAGPVGLLCASVSRAFGASTVVVVDINSDRLSVAQKYGATHTYKMSNESPEHNAARILEEMELDNGAHIVLDATGAEPCMNCGISVLASGGTFVQVGLGKPNPSLPVGQICDKEAIFRGSFRYGPGDYRTAIGLLSSGRVVLEGLVTHEFPFTQAEEAFKNVGNRQGIKTVIYGPGADENAAKATLT
>biolip__5vm2A Crystal structure of eck1772, an oxidoreductase/dehydrogenase of unknown specificity involved in membrane biogenesis from escherichia coli
MKNSKAILQVPGTMKIISAEIPVPKEDEVLIKVEYVGICGSDVHGFESGPFIPPKDPNQEIGLGHECAGTVVAVGSRVRKFKPGDRVNIEPGVPCGHCRYCLEGKYNICPDVDFMATQPNYRGALTHYLCHPESFTYKLPDNMDTMEGTLVEPAAVGMHAAMLADVKPGKKIIILGAGCIGLMTLQACKCLGATEIAVVDVLEKRLAMAEQLGATVVINGAKEDTIARCQQFTEDMGADIVFETAGSAVTVKQAPYLVMRGGKIMIVGTVPGASAINFLKINREVTIQTVFRYANRYPVTIEAISSGRFDVKSMVTHIYDYRDVQQAFEESVNNKRDIIKGVIKISD
>ecocyc__G6961-MONOMER putative zinc-binding dehydrogenase YdjJ (Escherichia coli K-12 substr. MG1655)
MKNSKAILQVPGTMKIISAEIPVPKEDEVLIKVEYVGICGSDVHGFESGPFIPPKDPNQEIGLGHECAGTVVAVGSRVRKFKPGDRVNIEPGVPCGHCRYCLEGKYNICPDVDFMATQPNYRGALTHYLCHPESFTYKLPDNMDTMEGALVEPAAVGMHAAMLADVKPGKKIIILGAGCIGLMTLQACKCLGATEIAVVDVLEKRLAMAEQLGATVVINGAKEDTIARCQQFTEDMGADIVFETAGSAVTVKQAPYLVMRGGKIMIVGTVPGDSAINFLKINREVTIQTVFRYANRYPVTIEAISSGRFDVKSMVTHIYDYRDVQQAFEESVNNKRDIIKGVIKISD
>BRENDA__A0A3S7PMB5 D-xylulose reductase (EC 1.1.1.9) (Pichia kudriavzevii)
MTIDPTLDLNNLKEDNPSVVLEKIGEIRFEERPVPEIPEPNYVKIAITHTGLCGSDVHYYEHGSCGSFKVESPMVLGHESAGIIVQVGDSVTRLKPGDRVACEPGVPSRLSKEYKAGNYNLCPHMAFAATPPYDGTLCRYYVLPEDFVVKLPDHVSLEEGALVEPLSVGVHANRLIDVKFGDSMVVFGAGPVGLLAAGVAKAFGCDKVLIVDIVNEKLDFAVQHKLATHCFNSKGKTFEDLLACIKDIWDEDELPTCGIDATGNQYCINMCIRSLAKKGRFVQVGMGGDTLDKFPIAAVLEKELTVKGSFRYSVDDYKYSVQLLKDGKINVRPLITHRFKFEQAVEAYEFSKQGKSIKIMIEGPP
>BRENDA__Q9HWM8 (R,R)-butanediol dehydrogenase (EC 1.1.1.4) (Pseudomonas aeruginosa)
MNSSPQANAAMRAAVWHGRHDIRVEDVPLPAEPPPGWVQIRVHWCGICGSDLHEYLAGPVFIPVEAPHPLTGLKDQCILGHEFSGEIVRLGNGVTGFAVGQAVAADACQHCGTCYYCRHGLYNICENLAFTGLMNNGAFAEYVNVPANLLYALPAGFPSEAGALIEPLAVGMHAVKKAGSLLGQNVVVVGAGTIGLSTIMCARAAGAAQVIALEMSSARKAKALEVGASQVLDPSRCDALGEIRALTGGLGADVSFECIGNKHTAKLAIDAIRKAGKCVLVGIFEEPSEFNFFELVSTEKQLLGALAYNGEFADVIAFIADGRLDIAPLVTGRIGLEEIVERGFEELVNNKEHNVKIIVSPGG
>SwissProt__Q763T4 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 (Aspergillus oryzae (Yellow koji mold))
MATATVLEKANIGVYTNTNHDLWVAESKPTLEEVKSGESLKPGEVTVQVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGEVIAVASDVTHLKPGDRVAVEPNIPCHACEPCLTGRYNGCEKVLFLSTPPVDGLLRRYVNHPAVWCHKIGDMSYEDGALLEPLSVSLAAIERSGLRLGDPVLVTGAGPIGLITLLSARAAGATPIVITDIDEGRLAFAKSLVPDVITYKVQTNLSAEDNAAGIIDAFNDGQGSAPDALKPKLALECTGVESSVASAIWSVKFGGKVFVIGVGKNEMKIPFMRLSTQEIDLQYQYRYCNTWPRAIRLVRNGVISLKKLVTHRFLLEDALKAFETAADPKTGAIKVQIMSNEEDVKGASA
>BRENDA__E1QSX6 2-dehydro-3-deoxy-L-rhamnonate dehydrogenase (NAD+) (EC 1.1.1.401) (Vulcanisaeta distributa)
MKALVWTAIKRMEVKDVEKPKPSLGWVLLRVRYTGICGSDVSGFLGLNELRKPPLIMGHEFTGVVEEVGPNVPKDIIGRLFAVNPIVGCGHCRYCKMGLKNLCIERKIIGIDYPGAYAEYVLAPYDNLYPVSDPVRGALAEPLATSLRAVRLSNASLGDSVLVLGAGPVGAFAIKLLSASGIRDLTVVEINKNRLEWARRFGATRLIEKSGDEALKEIKELYPEGVDVVIDAVGSESTRRLAINAVRRGGRIIFVGLHDNEVKIPGNVIVRNEIEIKGSFSYTDEDFRRSVNLLEQGLLDPREGWVDIRPLERGQESFEELTGTYTRYVKIMLTPGE
>BRENDA__H6WCP4 L-arabinitol 4-dehydrogenase (EC 1.1.1.12) (Aspergillus tubingensis)
MATATVLEKANIGVFTNTKHDLWVADAKPTLEEVKNGQGLQPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGQVVAVAPDVTSLKPGDRVAVEPNIICNACEPCLTGRYNGCENVQFLSTPPVDGLLRRYVNHPAIWCHKIGDMSYEDGALLEPLSVSLAGIERSGLRLGDPCLVTGAGPIGLITLLSARAAGASPIVITDIDEGRLEFAKSLVPDVRTYKVQTGLSAEQNAEGIINVFNDGQGSGPGALRPRIAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMTVPFMRLSTWEIDLQYQYRYCNTWPRAIRLVRNGVIDLKKLVTHRFLLEDAIKAFETAANPKTGAIKVQIMSSEDDVKAASAGQKI
>metacyc__MONOMER-13195 <small>L</small>-arabinitol 4-dehydrogenase (EC 1.1.1.9; EC 1.1.1.12) (Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513))
MATATVLEKANIGVFTNTKHDLWVADAKPTLEEVKNGQGLQPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGQVVAVAPDVTSLKPGDRVAVEPNIICNACEPCLTGRYNGCENVQFLSTPPVDGLLRRYVNHPAIWCHKIGDMSYEDGALLEPLSVSLAGIERSGLRLGDPCLVTGAGPIGLITLLSARAAGASPIVITDIDEGRLEFAKSLVPDVRTYKVQIGLSAEQNAEGIINVFNDGQGSGPGALRPRIAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMTVPFMRLSTWEIDLQYQYRYCNTWPRAIRLVRNGVIDLKKLVTHRFLLEDAIKAFETAANPKTGAIKVQIMSSEDDVKAASAGQKI
>biolip__7y9pA Xylitol dehydrogenase s96c/s99c/y102c mutant(thermostabilized form) from pichia stipitis
TANPSLVLNKIDDISFETYDAPEISEPTDVLVQVKKTGICGSDIHFYAHGRIGNFVLTKPMVLGHESAGTVVQVGKGVTSLKVGDNVAIEPGIPCRFCDECKSGHYNLCPHMAFAATPNEPNPPGTLCKYFKSPEDFLVKLPDHVSLELGALVEPLSVGVHASKLGSVAFGDYVAVFGAGPVGLLAAAVAKTFGAKGVIVVDIFDNKLKMAKDIGAATHTFNSKTGGSEELIKAFGGNVPNVVLECTGAEPCIKLGVDAIAPGGRFVQVGNAAGPVSFPITVFAMKELTLFGSFRYGFNDYKTAVGIFDTNYQNGRENAPIDFEQLITHRYKFKDAIEAYDLVRAGKGAVKCLIDGP
>biolip__4ej6A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021
QSMMKAVRLESVGNISVRNVGIPEPGPDDLLVKVEACGICGTDRHLLHGEFPSTPPVTLGHEFCGIVVEAGSAVRDIAPGARITGDPNISCGRCPQCQAGRVNLCRNLRAIGIHRDGGFAEYVLVPRKQAFEIPLTLDPVHGAFCEPLACCLHGVDLSGIKAGSTVAILGGGVIGLLTVQLARLAGATTVILSTRQATKRRLAEEVGATATVDPSAGDVVEAIAGPVGLVPGGVDVVIECAGVAETVKQSTRLAKAGGTVVILGVLPQGEKVEIEPFDILFRELRVLGSFINPFVHRRAADLVATGAIEIDRMISRRISLDEAPDVISNPAAAGEVKVLVIPS
>PDB_4ejm_A Crystal structure of a putative zinc-binding dehydrogenase (target psi-012003) from sinorhizobium meliloti 1021 bound to NADP
QSMMKAVRLESVGNISVRNVGIPEPGPDDLLVKVEACGICGTDRHLLHGEFPSTPPVTLGHEFCGIVVEAGSAVRDIAPG
ARITGDPNISCGRCPQCQAGRVNLCRNLRAIGIHRDGGFAEYVLVPRKQAFEIPLTLDPVHGAFCEPLACCLHGVDLSGI
KAGSTVAILGGGVIGLLTVQLARLAGATTVILSTRQATKRRLAEEVGATATVDPSAGDVVEAIAGPVGLVPGGVDVVIEC
AGVAETVKQSTRLAKAGGTVVILGVLPQGEKVEIEPFDILFRELRVLGSFINPFVHRRAADLVATGAIEIDRMISRRISL
DEAPDVISNPAAAGEVKVLVIP
>SwissProt__O58389 L-threonine 3-dehydrogenase; L-ThrDH; TDH; L-threonine dehydrogenase; EC 1.1.1.103 (Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3))
MSEKMVAIMKTKPGYGAELVEVDVPKPGPGEVLIKVLATSICGTDLHIYEWNEWAQSRIKPPQIMGHEVAGEVVEIGPGVEGIEVGDYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGVFAEYAVVPAQNIWKNPKSIPPEYATLQEPLGNAVDTVLAGPISGKSVLITGAGPLGLLGIAVAKASGAYPVIVSEPSDFRRELAKKVGADYVINPFEEDVVKEVMDITDGNGVDVFLEFSGAPKALEQGLQAVTPAGRVSLLGLYPGKVTIDFNNLIIFKALTIYGITGRHLWETWYTVSRLLQSGKLNLDPIITHKYKGFDKYEEAFELMRAGKTGKVVFMLK
>BRENDA__Q6KAV2 D-xylulose reductase (EC 1.1.1.9) (Blastobotrys adeninivorans)
MAAQVEEQVLNLRAQADHNPSFVLKKPLELGFEERPVPVITDPRDVKIQVKKTGICGSDVHFWQHGRIGDYVVEKPMVLGHESSGVVVEVGSEVTSLKVGDRVAMEPGVPDRRSKEYKMGRYHLCPHVRFAACPPTDGTLCKYYTLPEDFCVKLPENVDFEEGALVEPLSVAVHTARLLGIYPGSKVVVFGAGPIGQLCIGVCKAFGASIIGAVDLFEQKLETAKEFGASHTYVPQKGDSHDETAHKILELLPNKQAPDVVIDASGAEQSINAGIELLERGGTFGQVAMGRTDYIQFAVSRMAMKEIRFQGVFRYTYGDYELATQLIGDGKIPVKKLVTHRRPFEKAEEAYELVKSGVAVKCIIDGPE
>biolip__2dfvA Hyperthermophilic threonine dehydrogenase from pyrococcus horikoshii
EKMVAIMKTKPGYGAELVEVDVPKPGPGEVLIKVLATSICGTDLHIYEWNEWAQSRIKPPQIMGHEVAGEVVEIGPGVEGIEVGDYVSVETHIVCGKCYACRRGQYHVCQNTKIFGVDTDGVFAEYAVVPAQNIWKNPKSIPPEYATLQEPLGNAVDTVLAGPISGKSVLITGAGPLGLLGIAVAKASGAYPVIVSEPSDFRRELAKKVGADYVINPFEEDVVKEVMDITDGNGVDVFLEFSGAPKALEQGLQAVTPAGRVSLLGLYPGKVTIDFNNLIIFKALTIYGITGRHLWETWYTVSRLLQSGKLNLDPIITHKYKGFDKYEEAFELMRAGKTGKVVFMLK
>SwissProt__Q8U259 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 (Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1))
MSEKMVAIMKTKPEYGAELVEVDVPKPGPGEVLIKILATSICGTDLHIYEWNEWAQTRIRPPQIMGHEVAGEVVEVGPGVEGIEVGDYVSVETHIVCGKCYACKRGQYHVCQNTKIFGVDTDGVFAEYAVVPAQNVWKNPKNIPPEYATLQEPLGNAVDTVLAGPIAGKSVLITGAGPLGLLGIAVAKASGAYPVIVSEPSEFRRNLAKKVGADYVINPFEEDVVKEVMDITDGNGVDVFLEFSGAPKALEQGLQAVTPAGRVSLLGLFPGKVSIDFNNLIIFKALTVYGITGRHLWETWYTVSRLLQSGKLNIDPIITHKYKGFDKYEEAFELMRAGKTGKVVFMLK
>reanno__Dino_3607129 D-xylulose reductase (EC 1.1.1.9) (Dinoroseobacter shibae DFL-12)
MARALVLEAARKLALRDIDLPDELGPEDVRIAIDTVGVCGSDVHYYTHGKIGPFVVKQPMVLGHEAAGIVTEIGAAVTHLALGDRVCMEPGIPNGSSKASKLGVYNVDPAVQFWATPPVHGCLTPSVVHPAAFTFKLPDHVSFAEGAMVEPFAIGMQAAAKARIKPGDVALVTGAGPIGVMVALAALAGGCAKVFVSDLVEDKLAIAAGYDNIHPILIPRDNPAEVLQEATEGWGADVVFECAGAAASIQAALEAAAPAGCVVWVGMPVDPVPVDIVLAQSRELRMETVFRYANMYDRAIALLASGKVDLKPLISATFPFEDSIAAFDRAVEARPTDVKIQIKMGAS
>SwissProt__C5J3R8 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 (Talaromyces emersonii (Thermophilic fungus) (Rasamsonia emersonii))
MAAGISLTKPNIGVYTNPNHDLWVADAKPTLEEVKSGSDLKPGQVTVEIRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGVVIAVAPDVKTLKPGDRVAIEPNIICNKCEPCLTGRYNGCEAVEFLSTPPVDGLLRRYVNHPAIWCHKIGDMSFEDGALLEPLSVALAGMDRAGVRLGDPVLVAGAGPIGLVTLLCVRAAGATPIVITDIDEGRLRFAKELVPEVRTYRVQTGLSAEENAAGILDALNDGNGSAPDAIRPRVAMECTGVESSVASAIWSVKFGGKVFVIGVGKNEMKVPFMRLSTWEIDLQYQYRYCNTWPKAIRLVKNGVINLKKLVTHRFPLEDAVKAFETAANPKTGAIKVQIMSSEEDIKAASGVNGASN
>biolip__4ilkA Crystal structure of short chain alcohol dehydrogenase (rspb) from e. Coli cft073 (efi target efi-506413) complexed with cofactor nadh
GSHMKSILIEKPNQLSIIEREIPTPSAGEVRVKVKLAGICGSDSHIYRGHNPYPRVIGHEFFGVIDAVGEGVESARVGERVAVDPVVSCGHCYPCSIGKPNVCTTLAVLGVHADGGFSEYAVVPAKNAWKIPEAVADQYAVMIEPFTIAANVTGHGQPTENDTVLVYGAGPIGLTIVQVLKGVYNVKNVIVADRIDERLEKAKESGADWAINNSQTPLGESFAEKGIKPTLIIDAACHPSILKEAVTLASPAARIVLMGFSSEPSEVIQQGITGKELSIFSSRLNANKFPVVIDWLSKGLIKPEKLITHTFDFQHVADAISLFELDQKHCCKVLLTF
>SwissProt__B6HI95 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 (Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) (Penicillium chrysogenum))
MASATVTKTNIGVYTNPKHDLWIADSSPTAEDINAGKGLKAGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHVLGHESAGQVLAVAPDVTHLKVGDRVAVEPNVICNACEPCLTGRYNGCVNVAFLSTPPVDGLLRRYVNHPAVWCHKIGDMSYEDGAMLEPLSVTLAAIERSGLRLGDPLLITGAGPIGLISLLSARAAGACPIVITDIDEGRLAFAKSLVPEVRTYKVEIGKSAEECADGIINALNDGQGSGPDALRPKLALECTGVESSVNSAIWSVKFGGKVFVIGVGKNEMTIPFMRLSTQEIDLQYQYRYCNTWPRAIRLIQNGVIDLSKLVTHRYSLENALQAFETASNPKTGAIKVQIMSSEEDVKAATAGQKY
>ecocyc__G6838-MONOMER putative zinc-binding dehydrogenase RspB (Escherichia coli K-12 substr. MG1655)
MKSILIEKPNQLAIVEREIPTPSAGEVRVKVKLAGICGSDSHIYRGHNPFAKYPRVIGHEFFGVIDAVGEGVESARVGERVAVDPVVSCGHCYPCSIGKPNVCTTLAVLGVHADGGFSEYAVVPAKNAWKIPEAVADQYAVMIEPFTIAANVTGHGQPTENDTVLVYGAGPIGLTIVQVLKGVYNVKNVIVADRIDERLEKAKESGADWAINNSQTPLGEIFTEKGIKPTLIIDAACHPSILKEAVTLASPAARIVLMGFSSEPSEVIQQGITGKELSIFSSRLNANKFPIVIDWLSKGLIKPEKLITHTFDFQHVADAISLFEQDQKHCCKVLLTFSE
>CharProtDB__CH_000557 (R,R)-butanediol dehydrogenase; EC 1.1.1.4 (Pseudomonas putida)
MNDLSHTHMRAAVWHGRNDIRVEQVPLPADPAPGWVQIKVDWCGICGSDLHEYVAGPVFIPVEAPHPLTGIQGQCILGHEFCGQIAKLGEGVEGFAVGDPVAADACQHCGTCYYCTHGLYNICERLAFTGLMNNGAFAELVNVPANLLYRLPQGFPPEAGALIEPLAVGMHAVKKAGSLLGQTVVVVGAGTIGLCTIMCAKAAGAAQVIALEMSSARKAKAKEVGATVVLDPSQCDALAQIRALTFGLGADVSFECIGNKHTAKLAIDTIRKAGKCVLVGIFEEPSEFNFFELVSTEKQVLGALAYNGEFADVIAFIADGRLDIRPLVTGRIGLEQIVELGFEELVNNKEENVKIIVSPGVR
>metacyc__MONOMER-124212 pentitolphosphate dehydrogenase Lmo2664 (EC 1.1.1.301) (Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e))
MRAAVLYENNVIKAEQIDEATCGKDQVRVEVKAVGICGSDIHKMQTRWKYPLPAVMGHEFAGVITEIGSEVTNVAMGDRVAGIPLEPCMECNYCKAGDFALCDNYRMVGSHFHGGFAENVVMKADNVISIGDLDFEEGAMIEPLAVSMHGVLGIQPRLGDTVIVFGIGTIGILVVQCLLLAGVKDIIAVDISDKKLADAREFGCKYTINPKNEDLKERVFAYTNGLGADIALECAGSKITQEQCLLVTKKKGKVGFLGIAYADVLLHEEAFENIFRRELTLKGFWNSYSAPFPGEEWRTSIEFVKQGRIKLKPLISHRYKLEETKEAFDMILSREHDYNKVMILPQKGDD
>CharProtDB__CH_122531 putative L-arabinitol 4-dehydrogenase (Emericella nidulans)
MATATVLEKPNIGVFTNPKHDLWVAESKPTLEEVKSGESLKPGEVTIEVRSTGICGSDVHFWHAGCIGPMIVTGDHILGHESAGDVIAVAPDVTSLKVGDRVAIEPNVICNACEPCLTGRYNGCEKVAFLSTPPVDGLLRRYVNHPAVWCHKIGDMSYEDGALLEPLSVSLAAVERSGLRLGDPCLITGAGPIGLITLLSARAAGATPLVITDIDEGRLKFAKELVPEVRTYKVEIGFSAEETAEGIINAFNDGQGAGPDALRPRIALECTGVESSVASAIWSVKFGGKVFVIGVGKNEMKIPFMRLSTQEIDLQYQYRYCNTWPRAIRLVKNGVINLQKLVTHRYALEDALKAFETAANPKTGAIKVQIMSSTADVEAASAGQKN
>biolip__3m6iA L-arabinitol 4-dehydrogenase
ASKTNIGVFTNPQHDLWISEASPSLESVQKGEELKEGEVTVAVRSTGICGSDVHFWKHGCIGPMIVECDHVLGHESAGEVIAVHPSVKSIKVGDRVAIEPQVICNACEPCLTGRYNGCERVDFLSTPPVPGLLRRYVNHPAVWCHKIGNMSYENGAMLEPLSVALAGLQRAGVRLGDPVLICGAGPIGLITMLCAKAAGACPLVITDIDEGRLKFAKEICPEVVTHKVERLSAEESAKKIVESFGGIEPAVALECTGVESSIAAAIWAVKFGGKVFVIGVGKNEIQIPFMRASVREVDLQFQYRYCNTWPRAIRLVENGLVDLTRLVTHRFPLEDALKAFETASDPKTGAIKVQIQSL
>SwissProt__Q7SI09 L-arabinitol 4-dehydrogenase; LAD; EC 1.1.1.12 (Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987))
MASSASKTNIGVFTNPQHDLWISEASPSLESVQKGEELKEGEVTVAVRSTGICGSDVHFWKHGCIGPMIVECDHVLGHESAGEVIAVHPSVKSIKVGDRVAIEPQVICNACEPCLTGRYNGCERVDFLSTPPVPGLLRRYVNHPAVWCHKIGNMSYENGAMLEPLSVALAGLQRAGVRLGDPVLICGAGPIGLITMLCAKAAGACPLVITDIDEGRLKFAKEICPEVVTHKVERLSAEESAKKIVESFGGIEPAVALECTGVESSIAAAIWAVKFGGKVFVIGVGKNEIQIPFMRASVREVDLQFQYRYCNTWPRAIRLVENGLVDLTRLVTHRFPLEDALKAFETASDPKTGAIKVQIQSLE
>metacyc__MONOMER-17186 2-deoxy-<i>scyllo</i>-inosamine dehydrogenase (EC 1.1.1.329) (Streptomyces kanamyceticus)
MKALVFHSPEKATFEQRDVPTPRPGEALVHIAYNSICGSDLSLYRGVWHGFGYPVVPGHEWSGTVVEINGANGHDQSLVGKNVVGDLTCACGNCAACGRGTPVLCENLQELGFTKDGACAEYMTIPVDNLRPLPDALSLRSACQVEPLAVALNAVSIAGVAPGDRVAVMGAGGIGLMLMQVARHLGGEVTVVSEPVAERRAVAGQLGATELCSAEPGQLAELVARRPELTPDVVLEASGYPAALQEAIEVVRPGGRIGLIGYRVEETGPMSPQHIAVKALTLRGSLGPGGRFDDAVELLAKGDDIAVEPLLSHEFGLADYATALDLALSRTNGNVRSFFNLRD
>biolip__3gfbA L-threonine dehydrogenase (tktdh) from the hyperthermophilic archaeon thermococcus kodakaraensis
EKMQAIMKTKPAYGAELVEVDVPKPGPGEVLIKVLATSICGTDLHIYEWNEWAQSRIKPPQIMGHEVAGEVVEVGPGVEDLQVGDYISVETHIVCGKCYACKHNRYHVCQNTKIFGVDMDGVFAHYAIVPAKNAWKNPKDMPPEYAALQEPLGNAVDTVLAGPIAGRSTLITGAGPLGLLGIAVAKASGAYPVIVSEPSEFRRKLAKKVGADYVVNPFEEDPVKFVMDITDGAGVEVFLEFSGAPKALEQGLKAVTPGGRVSLLGLFPREVTIDFNNLIIFKALEVHGITGRHLWETWYTVSSLIQSGKLNLDPIITHKYKGFDKFEEAFELMRAGKTGKVVFFPHK
>SwissProt__Q5JI69 L-threonine 3-dehydrogenase; TDH; L-threonine dehydrogenase; EC 1.1.1.103 (Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)))
MAEKMQAIMKTKPAYGAELVEVDVPKPGPGEVLIKVLATSICGTDLHIYEWNEWAQSRIKPPQIMGHEVAGEVVEVGPGVEDLQVGDYISVETHIVCGKCYACKHNRYHVCQNTKIFGVDMDGVFAHYAIVPAKNAWKNPKDMPPEYAALQEPLGNAVDTVLAGPIAGRSTLITGAGPLGLLGIAVAKASGAYPVIVSEPSEFRRKLAKKVGADYVVNPFEEDPVKFVMDITDGAGVEVFLEFSGAPKALEQGLKAVTPGGRVSLLGLFPREVTIDFNNLIIFKALEVHGITGRHLWETWYTVSSLIQSGKLNLDPIITHKYKGFDKFEEAFELMRAGKTGKVVFFPHKG
>metacyc__MONOMER-13196 D-galactitol dehydrogenase (EC 1.1.1.12) (Hypocrea jecorina)
MSPSAVDDAPKATGAAISVKPNIGVFTNPKHDLWISEAEPSADAVKSGADLKPGEVTIAVRSTGICGSDVHFWHAGCIGPMIVEGDHILGHESAGEVIAVHPTVSSLQIGDRVAIEPNIICNACEPCLTGRYNGCEKVEFLSTPPVPGLLRRYVNHPAVWCHKIGNMSWENGALLEPLSVALAGMQRAKVQLGDPVLVCGAGPIGLVSMLCAAAAGACPLVITDISESRLAFAKEICPRVTTHRIEIGKSAEETAKSIVSSFGGVEPAVTLECTGVESSIAAAIWASKFGGKVFVIGVGKNEISIPFMRASVREVDIQLQYRYSNTWPRAIRLIESGVIDLSKFVTHRFPLEDAVKAFETSADPKSGAIKVMIQSLD
>BRENDA__G3AIP8 D-xylulose reductase (EC 1.1.1.9) (Spathaspora passalidarum)
MVANPSLVLKKIDEIVFENQEAPTITEPTDVIVQVKKTGICGSDIHFYQHGKIGNYILTKPMVLGHESAGVVTEVGPGVKYLRVGDNVAIEPGVPSRFSDAYKSGRYNLCPHMRFAATPSTKDEPNPPGTLCKYFKSPEDFLVKLPDHVSLELGAMVEPLSVGVHACKIGKVKFGDTVAVFGAGPVGLLTAATAKTFGAAKVIIIDVFDNKLQMAKDIGVVTHTFNSKTDGDYNDLIKHFGGQPNVVLECTGADPCVGMGVNICAPGGTFIQVGNAAAPVKFPITQFAMKELTLYGSFRYGFGDYQDAVNIFDANYKNGKDKAPIDFERLITHRFKFDDAIKAYDLVRSGCGAVKCLIDGPE
>BRENDA__G3AIB3 D-xylulose reductase (EC 1.1.1.9) (Spathaspora passalidarum)
MVANPSLVLNKIDDITFETYEAPEIVEPTDVIVEVKKTGICGSDIHYYAHGKIGNFILTKPMVLGHESAGVVSQVGKGVKHLKVGDRVAIEPGIPSRLSDAYKSGHYNLCPHMCFAATPNSTEGEPNPPGTLCKYFKSPEDFLVKLPEHVSLELGAMVEPLSVGVHASKLGKVTFGDNVAVFGAGPVGLLAAATAKTFGAARVIVIDIFDNKLQMAKDIGAATHTFNSKTGGDYKDLIAAFDGVEPNVILECTGAEPCIAMGVQIAAPGGRFVQVGNAGAAVKFPITEFATKELTLFGSFRYGYGDYQTAVNIFDANYKNGKDKAPIDFEQLITHRFKFDDAIKAYDLVRAGSGAVKCLIDGPL
>SwissProt__Q15SS1 2-dehydro-3-deoxy-L-galactonate 5-dehydrogenase; 2-keto-3-deoxy-L-galactonate 5-dehydrogenase; EC 1.1.1.389 (Pseudoalteromonas atlantica (strain T6c / ATCC BAA-1087))
MFAAQYIGNKSFNVVEGHAIAPQAGEVRLDVGYVGICGTDMHIYHGVMDQRVSIPQTIGHEISGVVAQIGEGVEGFTVGEKVVVRPLDWCGECPTCEAGLTHICQNLKFMGIDTPGAFQSSWTVKARTLHKLPAGVDLKQGALVEPLSVACHDVRRSRLKAGEKAVILGGGPIGQLVAAVAKSVGAEVLVSEPNDSRREFADELGVKSVNPMDTDLAAYVDQWTGTKGADVVFEVSGVLPAIQSMTQIAGRRGRIVMVAIHSTAPPIDLFQFFWKELELLGARVYEAADFDWAIELIASGQIDLKPFISSVSPLADIGSAFANMDGNPQGMKALVECNAEQ
>BRENDA__M5AJW4 coniferyl-alcohol dehydrogenase (EC 1.1.1.194); aryl-alcohol dehydrogenase (EC 1.1.1.90) (Streptomyces sp.)
MAQEVRGVIAPGKDEPVRMETILVPDPGPGEAVVQVQACGVCHTDLHYKQGGISDDFPFLLGHEAAGVVESVGDGVTDVAPGDFVILNWRAVCGQCRACLRGRPWYCFDTHNAEQKMTLASTGQELSPALGIGAFAEKTLVAAGQCTKVDPAVSAQVAGLLGCGVMAGIGAAINTGNVGRGDTVAVIGCGGVGDAAIAGANLAGAAKIIAVDIDDRKLETARGMGATHTVNSRTNDPVEAIRELTGGFGADVVIEAVGRPETYKQAFYARDLAGTVVLVGVPTPEMKLELPLLDVFGRGGALKSSWYGDCLPSRDFPMLIDLHLQGRLDLEAFVTETIELTDVEKAFERMHHGDVLRSVVVL
>ecocyc__THREODEHYD-MONOMER threonine dehydrogenase (EC 1.1.1.103) (Escherichia coli K-12 substr. MG1655)
MKALSKLKAEEGIWMTDVPVPELGHNDLLIKIRKTAICGTDVHIYNWDEWSQKTIPVPMVVGHEYVGEVVGIGQEVKGFKIGDRVSGEGHITCGHCRNCRGGRTHLCRNTIGVGVNRPGCFAEYLVIPAFNAFKIPDNISDDLAAIFDPFGNAVHTALSFDLVGEDVLVSGAGPIGIMAAAVAKHVGARNVVITDVNEYRLELARKMGITRAVNVAKENLNDVMAELGMTEGFDVGLEMSGAPPAFRTMLDTMNHGGRIAMLGIPPSDMSIDWTKVIFKGLFIKGIYGREMFETWYKMAALIQSGLDLSPIITHRFSIDDFQKGFDAMRSGQSGKVILSWD
>reanno__HerbieS_HSERO_RS17015 sorbitol dehydrogenase (EC 1.1.1.14); xylitol dehydrogenase (EC 1.1.1.9) (Herbaspirillum seropedicae SmR1)
MQALVLEATRELKLREIDLPQQMGAQDVRIRIHTVGICGSDLHYYTHGSIGPFKVEAPMVLGHEASGTVIEVGSAVSHLKVGDRVCMEPGIPRLDSPATLRGMYNLDPAVRFWATPPIHGCLTGSVVHPAAFTYRLPDNVSFAEGAIVEPLSIGLQAATKARMKPGDTAVVIGAGTIGAMTALAALAGGAARVILADVVAEKLAHFADNPAVITVDVTRETLTDVVRQATDGWGADVVFEASGHAGVYQTLLDLVCPGGCAVLVGMPPAPVALDVVAMQTKEVRLESVFRYANIFPRALALISSGMIDVKPFISRKFPFSQSIRAFEEAASGRPQDVKIQIEMEG
>BRENDA__E7EKB8 (R,R)-butanediol dehydrogenase (EC 1.1.1.4) (Paenibacillus polymyxa)
MQALRWHGVKDLRLENIEQPAALPGKVKIKVEWCGICGSDLHEYVAGPIFIPENAQHPLTGEKAPIVMGHEFSGQVVEIGEGVTKIQVGDRVVVEPVFACGECDACRQGKYNLCDKMGFLGLAGGGGGFSEYVAADEHMVHKIPESVSFEQGALVEPSAVALYAVRQSQLKVGDKAVVFGAGPIGLLVIEALKASGASEIYAVELSEERKAKAEELGAIVLDPKTYDVVEELHKRTNGGVDVAYEVTGVPPVLTQAIESTKISGQIMIVSIFEKEAPIKPNNIVMKERNLTGIIGYRDVFPAVISLMEKGYFPADKLVTKRIKLEEVIEQGFEGLLKEKNQVKILVSPKA
>metacyc__MONOMER-17231 2-deoxy-<i>scyllo</i>-inosamine dehydrogenase (EC 1.1.1.329) (Streptomyces fradiae)
MKALVFEAPERAVLTHRDIPAPAPGEALVRVAYNSVCGSDLSFYKGVWHGFTYPVVPGHEWSGSVVDVNGPRGADLVGRNVVGDLTCSCGTCAHCAAGTPTLCEDLGELGFTRDGACAEYMTVPVANLRPLPDTLPLRTACQVEPLAVALNAVDRLGVTPGEKVAVMGAGGIGLLLVQAVRLRGGTVTAVAEPVPERRAAALALGVPAAVGGDPGALVELTRSDPAAVPDVVLEASGYPTAVQEAVEAVRPGGRVGLVGYRIEEAAVMAPHHIVLKVLTVRASMGPGTRFEEAVDVLASGAVDVDALLSHEFALDDYAKALDVALRRADGNTRSYFNLRA