>GFF2389 FitnessBrowser__psRCH2:GFF2389
MTFETLLVDIQERVALITLNRPQALNALNGQLISELNQALGQLEADPQIGCIVLTGSAKAFAAGADIKEMAELTYPQIYLDDFFADADRIATRRKPLIAAVAGYALGGGCELALLCDMIFAADNARFGQPEVNLGVLPGIGGTQRLTRAVGKAKAMDMCLTGRQMDAAEAERAGLVARVFPAESLLEETLKAARVIAEKSLPATMMIKESVNRAFETTLAEGIRFERRVFHAVFATADQKEGMAAFSEKRKPEFTNR
>biolip__3h81A Crystal structure of enoyl-coa hydratase from mycobacterium tuberculosis
TYETILVERDQRVGIITLNRPQALNALNSQVMNEVTSAATELDDDPDIGAIIITGSAKAFAAGADIKEMADLTFADAFTADFFATWGKLAAVRTPTIAAVAGYALGGGCELAMMCDVLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLILTGRTMDAAEAERSGLVSRVVPADDLLTEARATATTISQMSASAARMAKEAVNRAFESSLSEGLLYERRLFHSAFATEDQSEGMAAFIEKRAPQFTHR
>PDB_3q0j_C Crystal structure of the mycobacterium tuberculosis crotonase in complex with the inhibitor acetoacetylcoa
MTYETILVERDQRVGIITLNRPQALNALNSQVMNEVTSAATELDDDPDIGAIIITGSAKAFAAGADIKEMADLTFADAFT
ADFFATWGKLAAVRTPTIAAVAGYALGGGCELAMMCDVLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLIL
TGRTMDAAEAERSGLVSRVVPADDLLTEARATATTISQMSASAARMAKEAVNRAFESSLSEGLLYERRLFHSAFATEDQS
EGMAAFIEKRAPQFT
>PDB_3q0g_C Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
MTYETILVERDQRVGIITLNRPQALNALNSQVMNEVTSAATELDDDPDIGAIIITGSAKAFAAGADIKEMADLTFADAFT
ADFFATWGKLAAVRTPTIAAVAGYALGGGCELAMMCDVLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLIL
TGRTMDAAEAERSGLVSRVVPADDLLTEARATATTISQMSASAARMAKEAVNRAFESSLSEGLLYERRLFHSAFATEDQS
EGMAAFIEKRAPQFT
>metacyc__MONOMER-21336 acryloyl-CoA hydratase (EC 4.2.1.116) (Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3))
MAFETIIVEVEDHVALIRLNRPDALNALNTQLLGELCTALEEADGNDKVRCIVITGSDKAFAAGADIREMSQKTYVEVYSENLFAAANDRVSAIRKPIIAAVAGYALGGGCELAMLCDFIIAADTAKFGQPEINLGVIAGIGGTQRLTRLVGKSKSMDLNLTGRFMDAEEAERAGLVSRVVPAKKLVEEALSAAQKIAEKSMISAYAVKEAVNRSYETTLSEGLLFERRVFHSMFATEDQKEGMAAFLEKRAAQFRDK
>reanno__Burk376_H281DRAFT_05725 2,3-dehydroadipyl-CoA hydratase / enoyl-CoA hydratase (EC 4.2.1.17) (Paraburkholderia bryophila 376MFSha3.1)
MVYENILVETRGRVGLVTLNRPKALNALNDALMDELGAALREFDADDAIGAIVLTGSEKAFAAGADIGMMSTYSYMDVYKGDYITRNWETVRSIRKPIIAAVAGFALGGGCELAMMCDMIFAADTAKFGQPEIKLGIMPGAGGTQRLPRAVSKAKAMDLCLTARFMDAAEAERAGLVSRVIPAASLIDEAIAAAATIAEFPLPAVMMVKESVNRAYETTLAEGVHFERRLFHSLFATEDQKEGMAAFVEKRKPVFKHR
>reanno__BFirm_BPHYT_RS17335 2,3-dehydroadipyl-CoA hydratase / enoyl-CoA hydratase (EC 4.2.1.17) (Burkholderia phytofirmans PsJN)
MAYENILVETRGRVGLVTLNRPKALNALNDALMDELGAALREFDADDAIGAIVVTGSEKAFAAGADIGMMSTYTYMDVYKGDYITRNWETVRSIRKPIIAAVAGFALGGGCELAMMCDIIFAADTAKFGQPEIKLGIMPGAGGTQRLPRAVSKAKAMDLCLTARFMDAAEAERAGLVSRVIPAASLVDEAIAAAATIAEFPSPAVMMVKESVNRAYETTLAEGVHFERRLFHSLFATEDQKEGMAAFVEKRKPVFKHR
>PDB_3q0g_D Crystal structure of the mycobacterium tuberculosis crotonase bound to a reaction intermediate derived from crotonyl coa
TYETILVERDQRVGIITLNRPQALNALNSQVMNEVTSAATELDDDPDIGAIIITGSAKAFAAGADIKEMFADAFTADFFA
TWGKLAAVRTPTIAAVAGYALGGGCELAMMCDVLIAADTAKFGQPEIKLGVLPGMGGSQRLTRAIGKAKAMDLILTGRTM
DAAEAERSGLVSRVVPADDLLTEARATATTISQMSASAARMAKEAVNRAFESSLSEGLLYERRLFHSAFATEDQSEGMAA
FIEKRAPQFT
>metacyc__MONOMER-15200 acryloyl-CoA hydratase/3-hydroxypropanoyl-CoA hydrolase (EC 3.1.2.4; EC 4.2.1.116) (Halomonas sp. HTNK1)
MIVVERRERVGLIILNRPKSLNALNRQLAEETLAVLREMDADPGIGAIVVTGNPRAFAAGADIEEMAEKSFTDFYMDDFLSPWDQVRQISKPIIAAVGGFALGGGCELALLCDFIIASDDAQFGQPEIKLGILPGIGGSQRLARSIGKAMTMDLVLTGRNIGAQEAKEIGLVARVVPKNDLMQHALEAAHTIAGYNEPAVKMAKSAVNAAFETPLAEGLRQERLLFQAAFATEGQKEGMSAFVKKRAPVFRHR
>metacyc__MONOMER-11697 short chain enoyl-CoA hydratase subunit (EC 4.2.1.150) (Bos taurus)
MAALRALLPRVRAPLRPWLFCPVQRSFASSAAFEYIITAKKGRNSNVGLIQLNRPKALNALCNGLIVELNQALQAFEEDPAVGAIVLTGGEKVFAAGADIKEMQSLTFQNCYSGGFLSHWDQLTRVKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETVVEEAIQCAEKIASNSKIVTAMAKESVNAAFEMTLAEGVKLEKKLFYSTFATEDRKEGMAAFVEKRKANFKDQ
>SwissProt__Q8BH95 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 (Mus musculus (Mouse))
MAALRALLPRACSSLLSSVRCPELRRFASGANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEQDPAVGAIVLTGGDKAFAAGADIKEMQNRTFQDCYSSKFLSHWDHITRVKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVEKLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGNKLEKRLFYSTFATDDRREGMTAFVEKRKANFKDH
>biolip__1dubA 2-enoyl-coa hydratase, data collected at 100 k, ph 6.5
ANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGKFLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKANFKDH
>PDB_1ey3_A Structure of enoyl-coa hydratase complexed with the substrate dac-coa
FQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDCY
SGKFLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMV
LTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDR
REGMSAFVEKRKANFKDH
>SwissProt__P14604 Enoyl-CoA hydratase, mitochondrial; mECH; mECH1; Enoyl-CoA hydratase 1; ECHS1; Short-chain enoyl-CoA hydratase; SCEH; EC 4.2.1.17; EC 5.3.3.8 (Rattus norvegicus (Rat))
MAALRALLPRACNSLLSPVRCPEFRRFASGANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDCYSGKFLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGMSAFVEKRKANFKDH
>PDB_2dub_A Enoyl-coa hydratase complexed with octanoyl-coa
NFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQDC
YSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMVLTGD
RISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDRREGM
SAFVEKRKANFKDH
>biolip__2hw5C The crystal structure of human enoyl-coenzyme a (coa) hydratase short chain 1, echs1
ANFEYIIAEKRGKNNTVGLIQLNRPKALNALCDGLIDELNQALKIFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
>PDB_1mj3_A Crystal structure analysis of rat enoyl-coa hydratase in complex with hexadienoyl-coa
ANFQYIITEKKGKNSSVGLIQLNRPKALNALCNGLIEELNQALETFEEDPAVGAIVLTGGEKAFAAGADIKEMQNRTFQD
CYSGLSHWDHITRIKKPVIAAVNGYALGGGCELAMMCDIIYAGEKAQFGQPEILLGTIPGAGGTQRLTRAVGKSLAMEMV
LTGDRISAQDAKQAGLVSKIFPVETLVEEAIQCAEKIANNSKIIVAMAKESVNAAFEMTLTEGNKLEKKLFYSTFATDDR
REGMSAFVEKRKANFKDH
>metacyc__HS05132-MONOMER short-chain enoyl-CoA hydratase monomer (EC 4.2.1.17) (Homo sapiens)
MAALRVLLSCVRGPLRPPVRCPAWRPFASGANFEYIIAEKRGKNNTVGLIQLNRPKALNALCDGLIDELNQALKTFEEDPAVGAIVLTGGDKAFAAGADIKEMQNLSFQDCYSSKFLKHWDHLTQVKKPVIAAVNGYAFGGGCELAMMCDIIYAGEKAQFAQPEILIGTIPGAGGTQRLTRAVGKSLAMEMVLTGDRISAQDAKQAGLVSKICPVETLVEEAIQCAEKIASNSKIVVAMAKESVNAAFEMTLTEGSKLEKKLFYSTFATDDRKEGMTAFVEKRKANFKDQ
>metacyc__MONOMER-943 BadK (Rhodopseudomonas palustris)
MSSNPILTETQGRVGIITLNRPDVLNALNDALMDALGGALLAFDADDGIGAIVIAGNTRAFAAGADIASMAAWSYSDVYGSNFITRNWETIRQIRKPVLAAVAGLAYGGGCELALACDIVIAGRSAKFALPEIKLGLLPGAGGTQRLPRAIGKAKAMDMCLSARPLNAEEADRYGLVSRVVDDDRLRDETVALATTIAAFSAPALMALKESLNRAFESTLAEGILFERRELHARFASADAREGIQAFLEKRAPCFSHR
>CharProtDB__CH_121974 mitochondrial enoyl-CoA hydratase (Emericella nidulans)
MFARQSTRFLFPRTTTVITRVRLYSSAAPSYEHILTSTPKPGVGLITLNRPKALNALSSPLFKEVNDALSKYDESKDIGAIIITGSEKAFAAGADIKEMAPLTFASAYSNNFIAPWSHLANSIRKPVIAAVSGFALGGGCELALMCDIIYCTASATFGQPEIKLGVIPGAGGSQRLTAAVGKSKAMELILTGKNFSGKEAGEWGVAAKVVDGGKEELLEEAVKTAETIAGYSRVATVAAKEVVNKSQDLGVREGVEYERRLFHGLFGSQDQKIGMTAFAEKKKPQWSHE
>metacyc__MONOMER-15953 2,3-dehydroadipyl-CoA hydratase (EC 4.2.1.17) (Pseudomonas sp. Y2)
MPHTLSVDAPEQGVRLITLQRPEALNALNTQLLDELAAELALAEQDAETRAVVLTGSRKAFAAGADIKEMAERDLVGILEDPRVAHWQRIAAFSKPLIAAVNGFCLGGGCELAMHADILIAGEDARFGQPEINLGIMPGAGGTQRLLRAVGKSLAMQMVLSGQAIDARHAQRAGLVSEVTLPELTIERALAIARVIAQKAPLAVRLAKEALLKAEDTDLASGLRFERHAFTVLAGTADRAEGIRAFQEKRRPEFTGR
>metacyc__MONOMER-13729 3-hydroxypropionyl-CoA dehydratase (EC 4.2.1.116) (Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2))
MEFETIETKKEGNLFWITLNRPDKLNALNAKLLEELDRAVSQAESDPEIRVIIITGKGKAFCAGADITQFNQLTPAEAWKFSKKGREIMDKIEALSKPTIAMINGYALGGGLELALACDIRIAAEEAQLGLPEINLGIYPGYGGTQRLTRVIGKGRALEMMMTGDRIPGKDAEKYGLVNRVVPLANLEQETRKLAEKIAKKSPISLALIKEVVNRGLDSPLLSGLALESVGWGVVFSTEDKKEGVSAFLEKREPTFKGK
>ecocyc__G6714-MONOMER putative 2,3-dehydroadipyl-CoA hydratase (EC 4.2.1.17) (Escherichia coli K-12 substr. MG1655)
MSELIVSRQQRVLLLTLNRPAARNALNNALLMQLVNELEAAATDTSISVCVITGNARFFAAGADLNEMAEKDLAATLNDTRPQLWARLQAFNKPLIAAVNGYALGAGCELALLCDVVVAGENARFGLPEITLGIMPGAGGTQRLIRSVGKSLASKMVLSGESITAQQAQQAGLVSDVFPSDLTLEYALQLASKMARHSPLALQAAKQALRQSQEVALQAGLAQERQLFTLLAATEDRHEGISAFLQKRTPDFKGR
>metacyc__MONOMER-13469 crotonase (EC 4.2.1.150) (Clostridium kluyveri (strain ATCC 8527 / DSM 555 / NCIMB 10680))
MEFKNIILEKDGNVASITLNRPKALNALNAATLKEIDAAINDIAEDDNVYAVIITGSGKAFVAGADIAEMKDLTAVEGRKFSVLGNKIFRKLENLEKPVIAAINGFALGGGCELSLSCDIRIASSKAKFGQPEVGLGITPGFGGTQRLARAIGVGMAKELIYTGKVINAEEALRIGLVNKVVEPDKLLEEAKALVDAIIVNAPIAVRMCKAAINQGLQCDIDTGVAYEAEVFGECFATEDRVEGMTAFVEKRDKAFKNK
>metacyc__CRTCLOS-MONOMER crotonase monomer (EC 4.2.1.74; EC 4.2.1.150) (Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787))
MELNNVILEKEGKVAVVTINRPKALNALNSDTLKEMDYVIGEIENDSEVLAVILTGAGEKSFVAGADISEMKEMNTIEGRKFGILGNKVFRRLELLEKPVIAAVNGFALGGGCEIAMSCDIRIASSNARFGQPEVGLGITPGFGGTQRLSRLVGMGMAKQLIFTAQNIKADEALRIGLVNKVVEPSELMNTAKEIANKIVSNAPVAVKLSKQAINRGMQCDIDTALAFESEAFGECFSTEDQKDAMTAFIEKRKIEGFKNR
>ENA__AAL09093.1 DcaE (Acinetobacter baylyi)
MIPDQDNFVEIDFSIEQIAIVKINRPASKNALNTEVRKQLAQAFTELSFNDQINAIVLTGGEDVFAAGADLKEMATASSTDMLLRHTERYWNAIAQCPKPVIAAVNGYALGGGCELAMHTDIIIAGKSATFGQPEIKVGLMPGAGGTQRLFRAVGKFHAMRMIMTGVMVPAEEAYLIGLVSQVTEDSQTIPTAIKMAQSLAKMPPIALQQIKEVALMSEDVPLNAGLTLERKSFQLLFSTEDKNEGINAFIEKRKPSYHGK
>SwissProt__Q0AVM1 Crotonyl-CoA hydratase; EC 4.2.1.150 (Syntrophomonas wolfei subsp. wolfei (strain DSM 2245B / Goettingen))
MAYENIILEKEEKLAVLYINRPKAMNALNKDTLLEIKDAVTAVNDDPAVELLIITGSGDKSFVAGADIAFMQNLSAMEAREFGALGQKVFRLIEAMEKPVIAAVNGFALGGGCELAMCCDFRIAASNAKFGQPEVGLGITPGFGGTQRLPRLVGPGMAKQLLYTADVINADEAFRIGLVNKVVQPEELLPEVKKIAGRILSKGQLAVRLSKAAANEGMQTDIDRAMSIEADAFGLCFATQDQKEGMTAFLEKRKANFISK
>metacyc__MONOMER-13738 crotonyl-CoA hydratase/(S)-3-hydroxybutyryl-CoA dehydrogenase (EC 1.1.1.35; EC 4.2.1.150) (Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2))
MKVTVIGSGVMGHGIAELAAIAGNEVWMNDISTEILQQAMERIKWSLSKLRESGSLKEGVEQVLARIHPETDQAQALKGSDFVIEAVKEDLELKRTIFRNAEAHASPSAVLATNTSSLPISEIASVLKSPQRVVGMHFFNPPVLMPLVEIVRGKDTSDEVVKTTAEMAKSMNKETIVVKDVPGFFVNRVLLRIMEAGCYLVEKGIASIQEVDSSAIEELGFPMGVFLLADYTGLDIGYSVWKAVTARGFKAFPCSSTEKLVSQGKLGVKSGSGYYQYPSPGKFVRPTLPSTSKKLGRYLISPAVNEVSYLLREGIVGKDDAEKGCVLGLGLPKGILSYADEIGIDVVVNTLEEMRQTSGMDHYSPDPLLLSMVKEGKLGRKSGQGFHTYAHEEAKYSTIVVRVEPPLAWIVLNRPTRYNAINGDMIREINQALDSLEEREDVRVIAITGQGRVFSAGADVTEFGSLTPVKAMIASRKFHEVFMKIQFLTKPVIAVINGLALGGGMELALSADFRVASKTAEMGQPEINLGLIPGGGGTQRLSRLSGRKGLELVLTGRRVKAEEAYRLGIVEFLAEPEELESEVRKLANAIAEKSPLAVASAKLAYKLGEETHIWTGTSLEASLFGLLFSTKDFEEGVRAFLEKRKPNFRGE
>BRENDA__F4JML5 methylglutaconyl-CoA hydratase (EC 4.2.1.18) (Arabidopsis thaliana)
MSFVKYLRRDNLLQLAGKPSLSRNYILQTCRTLIIETSPPEFVKLNRLSGSDSGIIEVNLDRPVTKNAINKEMLKSLQNAFESIHQDNSARVVMIRSLVPGVFCAGADLKERRTMSPSEVHTYVNSLRYMFSFIEALSIPTIAAIEGAALGGGLEMALACDLRICGENAVFGLPETGLAIIPGAGGTQRLSRLVGRSVSKELIFTGRKIDAIEAANKGLVNICVTAGEAHEKAIEMAQQINEKGPLAIKMAKKAIDEGIETNMASGLEVEEMCYQKLLNTQDRLEGLAAFAEKRKPLYTGN
>metacyc__MONOMER-688 (2S)-2-[(R)-hydroxybenzyl]succinyl-CoA monomer (EC 4.2.1.180) (Thauera aromatica)
MPVTLEVSNHVAYVTLNRPEAMNSLDPESTADLTEIWARVRTDPDIRVAVLTGAGEKSFCTGTDMKKSPPPTECMAATYLRDGQPILPHMKMWKPIIAAINGYAVGGGLEIALACDLRIASTNAKFGLTEVKVASLAGLNGTQALPRAIPQAVAMKMLLTGEMISAEEALRYGLVSDVVEPSALADLARSYAEKIASAAPLSVQATKQAAVLGKDMPLEHGILYSHLLWGVLRDTEDRKEGFKAFGERRAPAFRGA
>BRENDA__D3RXI4 3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35); 3-hydroxybutyryl-CoA dehydratase (EC 4.2.1.55) (Ferroglobus placidus)
MEVKNIAVLGAGAMGHAIAELAAVSGFNVKIRDIKEEILKNAMERIKQSLEKDFKKGRLKEDPQAVLSRITATLDLKEAVEDADMIIEAIPEIMDLKKQVFAECEEYCREDTIIATNTSSLSITELSKALKKPERFIGLHFFNPPKVMRLVEIVWGEKTSEETVKITEEVARKMNRVIIHVRKDVPGFVVNRIFVTMANEAAWALEKGEGSVEEIDSAVKYRMGLPMGLFELHDLLGGGCIDVSYHVLEYFRQTLGESYRPAPPFERLFKAGHLGKKSGKGFYDWSEGKSNEVPLRAGANFDLLRLIAPAVNEAAWLIEKEVATAEEIDLGVIHGLNYPRGLLRMADDIGIDKIVEKLEKLYEEYGEERYKVNPVLQKMVEENKLGRKTGEGFYKYGRGLYEFVKVEKPKENVAVIKLNRPQRANALNETFLKELEDALEWLEEDENVRCIVITGEGRNFCAGADIAVFAEGKVERMFEFSQLGQKVFNKIEKLSKPVIAAVNGAAMGGGFELALACDLRVVSSRAILALPELNLGIFPGWGGTQRLALAVGVSKAKQLIFMRENIDAKTAYDLGIANYIAEENEFWDKVMEVAEKIAEGPPLAYKFTKRVMFHGIKPELEASLFMESAAGGDIVLSDDVAEGIQAFSYRRKPNFKGR
>SwissProt__G4V4T7 Enoyl-CoA-hydratase; EC 4.2.1.17 (Amycolatopsis orientalis (Nocardia orientalis))
MSETRVRYEKKDHVAYVTMDRPAVLNAMDRRMHEELAGIWDDVEADDDVRAVVLTGAGDRAFSVGQDLKERARLNESGVAPTTFGSGGQAGHPRLTDRFTLSKPVVARVRGYALGGGFELVLACDIVIAAEDAVFALPEVRLGLIAGAGGVFRLPRQLPQKVAMGYLLTGRRMDAATALRHGLVNEVVPAAELDQCVADWTDSLVRAAPLSVRAIKEAALRSVDLPLEEAFTTSYHWEERRRRSADAIEGVRAFAEKRDPIWTGQ
>SwissProt__P94549 Probable enoyl-CoA hydratase; EC 4.2.1.17 (Bacillus subtilis (strain 168))
MNAISLAVDQFVAVLTIHNPPANALSSRILEELSSCLDQCETDAGVRSIIIHGEGRFFSAGADIKEFTSLKGNEDSSLLAERGQQLMERIESFPKPIIAAIHGAALGGGLELAMACHIRIAAEDAKLGLPELNLGIIPGFAGTQRLPRYVGTAKALELIGSGEPISGKEALDLGLVSIGAKDEAEVIEKAKALAAKFAEKSPQTLASLLELLYSNKVYSYEGSLKLEAKRFGEAFESEDAKEGIQAFLEKRKPQFKGE
>biolip__5jbxB Crystal structure of liuc in complex with coenzyme a and malonic acid
GPHMPEFKVDARGPIEIWTIDGESRRNAISRAMLKELGELVTRVSSSRDVRAVVITGAGDKAFCAGADLKERATMAEDEVRAFLDGLRRTFRAIEKSDCVFIAAINGAALGGGTELALACDLRVAAPAAELGLTEVKLGIIPGGGGTQRLARLVGPGRAKDLILTARRINAAEAFSVGLANRLAPEGHLLAVAYGLAESVVENAPIAVATAKHAIDEGTGLELDDALALELRKYEEILKTEDRLEGLRAFAEKRAPVYKGR
>BRENDA__Q1D5Y4 methylglutaconyl-CoA hydratase (EC 4.2.1.18) (Myxococcus xanthus)
MPEFKVDARGPIEIWTIDGESRRNAISRAMLKELGELVTRVSSSRDVRAVVITGAGDKAFCAGADLKERATMAEDEVRAFLDGLRRTFRAIEKSDCVFIAAINGAALGGGTELALACDLRVAAPAAELGLTEVKLGIIPGGGGTQRLARLVGPGRAKDLILTARRINAAEAFSVGLANRLAPEGHLLAVAYGLAESVVENAPIAVATAKHAIDEGTGLELDDALALELRKYEEILKTEDRLEGLRAFAEKRAPVYKGR
>BRENDA__Q8GB17 crotonobetainyl-CoA hydratase (EC 4.2.1.149) (Proteus sp.)
MSQSLHLTTRGSVLEIILDRPKANAIDAKTSHEMGEVFMRFRDDPSLRVAIITGAGERFFCAGWDLKAAAEGEAPDADFGAGGFAGLTELFDLNKPVIAAINGYAFGGGFELALAADMIICSDNASFALPEAQLGIVPDSGGVLRLPKRLPPAIVNEMLMTGRRMNAQEALRWGIANRVVSATELMDSARELADQIANSAPLAVAALKEIYRATSELSIEEGYKLMRSGVLKYYPRVLHSEDALEGPLAFAEKRSPEWKGR
>metacyc__MONOMER-21975 enoyl-CoA hydratase (EC 4.2.1.17) (Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337))
MTASVLYQASEGVATLTLNRPDVLNAMNGDLMRELREGVERAAGDAGVRAVLITGAGRGFCAGADLAARGKDGISDSGTLLRERYHPIIMALRQMPKPVVTAVNGVAAGAGMSLALAGDVVLAARSASFLQAFSKIGLVPDAGSTYFVPRYAGEMRARALAILAEKIDAEEAQRIGLVWKVHADDALQDEAGKLARHLATMPTMAYGMIKEALNQSFDNDLAAQLEVEATLQSRASRSDDCKEGVAAFMEKRKPQFKGR
>SwissProt__A0A481WNM8 Enoyl-CoA isomerase/hydratase claC; Clavatol biosynthesis cluster protein C; EC 4.2.1.- (Penicillium crustosum (Blue mold fungus))
MERSFTVECPPFEVEISHWDRILPPTHSKRILCFSLPETTDKEKVVEQLHIAFHHTVQRLPLLAGSVVPFSSHQGGRPWLRNIIPEGGAQLIVKDLSEELRFSDLAKTNFSQHLLNTEQLCPLPEVGYFKNESVDVCRFQANFIEGGLLLVVSIIHNAADGRGVTEVIKIFANELSKAQSGETHYPLEPRPDVYRTDRTKLVSGHGVPGSIENHAAWTSDPANAHAQIHNVENSCRTFRISVKALSDLKKSLSATSRGPDEWFSTNDAISAFIWRSIMLARHRAGILNGDAETYVAQPVDCRPHLEIPMPYFGNVIYMTKSSVPLSDLADFESGLGAAARALRADIKGVTAEKFRDLVGYAERTALETHTRLNILEAMSTSGIILTSLFKMDLHGMNFGPIFGDGHIKALRLPARGTQAGAVIVLPRVPDGSCEFMVTEQESTIKCLLEDEYFSRFTNDADSIGASSEEVVAPLPQPPITSEEGMISIDSTPPVIEAITIKSAPDIEPVTIEAATTEVEPITIKSISDTETVTIGITTTEVGPASTEATSPVVEPSTMESDLVEPVTVGTTNSEVESVTTETTASKVQALTTISKEWHLVPAGDVKMPSTLISNRIDAPQVGTIKIIQLNRPAAKNALSVQMVHELSCEIEEIHNERHMGGTRALVIASAVDGVFCAGADLKERKDMSLTETQAFLTSLRGLYSRLAALPIPTIACVSGHALGGGLELALCCHLRVFASNAVAALPETRLAIIPGAGGTYRLPNIVGMSNALDMILTGRGVPASEAAKMGLCNRLVGADGSEDTQAFSNRVLALETGIQLAEQISDAGPIAIRAAIRALSYSCEAVENAAYESVLTTKDRKAALAAFSEKRKPILVGE
>metacyc__MONOMER-18320 cyclohexa-1,5-dienecarbonyl-CoA hydratase monomer (EC 4.2.1.100) (Syntrophus aciditrophicus (strain SB))
MGFNTILFEKKDKVATITLNVPNSNWLTIPMMKEINEALMDVKKDPTIQLLVFDHAGDKAFCDGVDVADHVPEKVDEMIDLFHGMFRNMAAMDVTSVCLVNGRSLGGGCELMAFCDIVIASEKAKIGQPEINLAVFPPVAAAWFPKIMGLKKAMELILTGKIISAKEAEAIGLVNVVLPVEGFREAAQKFMADFTSKSRPVAMWARRAIMAGLNLDFLQALKASEIIYMQGCMATEDANEGLASFLEKRKPVFKDK
>biolip__6slbAAA 6slbAAA
NIGMILKERQDGVLVLTLNRPEKLNAITGELLDALYAALKEGEEDREVRALLLTGAGRAFSAGQDLTEFGDRKPDYEAHLRRYNRVVEALSGLEKPLVVAVNGVAAGAGMSLALWGDLRLAAVGASFTTAFVRIGLVPDSGLSFLLPRLVGLAKAQELLLLSPRLSAEEALALGLVHRVVPAEKLMEEALSLAKELAQGPTRAYALTKKLLLETYRLSLTEALALEAVLQGQAGQTQDHEEGVRAFREKRPPRFQGR
>BRENDA__Q5SLK3 2-(1,2-epoxy-1,2-dihydrophenyl)acetyl-CoA isomerase (EC 5.3.3.18) (Thermus thermophilus)
MVLKERQDGVLVLTLNRPEKLNAITGELLDALYAALKEGEEDREVRALLLTGAGRAFSAGQDLTEFGDRKPDYEAHLRRYNRVVEALSGLEKPLVVAVNGVAAGAGMSLALWGDLRLAAVGASFTTAFVRIGLVPDSGLSFLLPRLVGLAKAQELLLLSPRLSAEEALALGLVHRVVPAEKLMEEALSLAKELAQGPTRAYALTKKLLLETYRLSLTEALALEAVLQGQAGQTQDHEEGVRAFREKRPPRFQGR
>ecocyc__CARNRACE-MONOMER crotonobetainyl-CoA hydratase (EC 4.2.1.149) (Escherichia coli K-12 substr. MG1655)
MSESLHLTRNGSILEITLDRPKANAIDAKTSFEMGEVFLNFRDDPQLRVAIITGAGEKFFSAGWDLKAAAEGEAPDADFGPGGFAGLTEIFNLDKPVIAAVNGYAFGGGFELALAADFIVCADNASFALPEAKLGIVPDSGGVLRLPKILPPAIVNEMVMTGRRMGAEEALRWGIVNRVVSQAELMDNARELAQQLVNSAPLAIAALKEIYRTTSEMPVEEAYRYIRSGVLKHYPSVLHSEDAIEGPLAFAEKRDPVWKGR
>PDB_6sla_AAA Enoyl-CoA hydratase/carnithine racemase
MILKERQDGVLVLTLNRPEKLNAITGELLDALYAALKEGEEDREVRALLLTGAGRAFSAGQDLTEAHLRRYNRVVEALSG
LEKPLVVAVNGVAAGAGMSLALWGDLRLAAVGASFTTAFVRIGLVPNSGLSFLLPRLVGLAKAQELLLLSPRLSAEEALA
LGLVHRVVPAEKLMEEALSLAKELAQGPTRAYALTKKLLLETYRLSLTEALALEAVLQGQAGQTQDHEEGVRAFREKRPP
RFQGR
>metacyc__MONOMER-18964 methylglutaconyl-CoA hydratase (EC 4.2.1.18) (Ustilago maydis (strain 521 / FGSC 9021))
MTASALAYLEPDSSAELTGVYHLVLDRPEARNAISRSLLQDVLQCLQVLVCKITQPKQDEPLPRVLILRANGPCFCAGADLKERREMSEAEVIEFLQDLRHMLEQVEKLPIPTLAAIDGPALGGGLELALACDFRIAAETVSKIGFPEVKLGIIPGAGGTQRAPRIIGMQRAKELIYTGTQLNATQAKDLGLIDHVAPGSTCLKLCQELAQQMMPSAPLALRAAKMAISMGANVELARGLDLEWACYEPLLESKDRREALDAFQQKRKPIFTGK
>metacyc__MONOMER-13812 naphthoyl-CoA synthase (EC 4.1.3.36) (Bacillus subtilis (strain 168))
MAEWKTKRTYDEILYETYNGIAKITINRPEVHNAFTPKTVAEMIDAFADARDDQNVGVIVLAGAGDKAFCSGGDQKVRGHGGYVGDDQIPRLNVLDLQRLIRVIPKPVVAMVSGYAIGGGHVLHIVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEQLEEETIKWCEEMLEKSPTALRFLKAAFNADTDGLAGIQQFAGDATLLYYTTDEAKEGRDSFKEKRKPDFGQFPRFP
>SwissProt__Q4WF54 Mevalonyl-coenzyme A hydratase sidH; Siderophore biosynthesis protein H; EC 4.2.1.- (Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 / Af293) (Neosartorya fumigata))
MSTEAHPTVQGCLVSFPTPHILLLTLNRPEKRNCISLATSAEIQRLWTWFDTQPALYVAIITGTGESFCAGADLKEWNDLNARGITNEMTAPGLAGLPRRRGSKPIIAAVNGYCLGGGFEMVANCDIVVASENATFGLPEVQRGIAAVAGSLPRLVRVLGKQRAAEIALSGLSFSASQLERWGLVNRVVEHDQLLATAVEIATAISRNSPDSVRVTMEGLHYGWEMASVEEASSALVDQWYAKLMAGENFHEGVRAFVEKRKPQWRPSKL
>PDB_4elw_A Structure of e. Coli. 1,4-dihydroxy-2- naphthoyl coenzyme a synthases (menb) in complex with nitrate
PDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNIGVIILTGAGDKAFC
SGGDQKHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGASYMARIVGQK
KAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFY
MTEEGQEGRNAFNQKRQPDFSKFKRNP
>SwissProt__Q5SKU3 Putative enoyl-CoA hydratase; TtECH; EC 4.2.1.17 (Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8))
MVQVEKGHVAVVFLNDPERRNPLSPEMALSLLQALDDLEADPGVRAVVLTGRGKAFSAGADLAFLERVTELGAEENYRHSLSLMRLFHRVYTYPKPTVAAVNGPAVAGGAGLALACDLVVMDEEARLGYTEVKIGFVAALVSVILVRAVGEKAAKDLLLTGRLVEAREAKALGLVNRIAPPGKALEEAKALAEEVAKNAPTSLRLTKELLLALPGMGLEDGFRLAALANAWVRETGDLKEGIRAFFEKRPPRF
>SwissProt__O53561 Enoyl-CoA hydratase EchA19; EC 4.2.1.- (Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv))
MATVESGPDALVERRGHTLIVTMNRPAARNALSTEMMRIMVQAWDRVDNDPDIRCCILTGAGGYFCAGMDLKAATQKPPGDSFKDGSYGPSRIDALLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLYPMGGSAVRLVRQIPYTLACDLLLTGRHITAAEAKEMGLIGHVVPDGQALTKALELADAISANGPLAVQAILRSIRETECMPENEAFKIDTQIGIKVFLSDDAKEGPRAFAEKRAPNFQNR
>SwissProt__A0R4Q3 Enoyl-CoA hydratase EchA19; EC 4.2.1.- (Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155) (Mycobacterium smegmatis))
MSETGKGPDALVEQRGHTLIVTLNRPEARNALSGEMLSIMVEAWDRVDNDPEIRTCILTGAGGYFCSGMDLKGADKKPPGDSFKDGSYDPSKIPGLLKGRRLTKPLIAAVEGPAIAGGTEILQGTDIRVAGESAKFGISEAKWSLYPMGGSAVRLVRQIPYTIACDMLLTGRHITAAEAKEYGLIGYVVPDGTALDKALEIAETINNNGPLAVQAILKTIRETEGMHEDEAFGPDTRNGIPVFLSEDAKEGPRAFKEKRAPNFQMK
>ENA__AAA50401.1 dihydroxynapthoic acid (DHNA) synthetase (Bacillus subtilis)
MKIFDETYNGIAKITINRPEVHNAFTPKTVAEMIDAFADARDDQNVGVIVLAGAGDKAFCSGGDQKVRGHGGYVGDDQIPRLNVLDLQRLIRVIPKPVVAMVSGYAIGGGHVLHIVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEQLEEETIKWCEEMLEKSPTALRFLKAAFNADTDGLAGIQQFAGDATLLYYTTDEAKEGRDSFKEKRKPDFGQFPRFP
>PDB_4elx_A Structure of apo e.Coli. 1,4-dihydroxy-2- naphthoyl coa synthases with cl
PDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNIGVIILTGAGDKAFC
SGGDQKHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGASYMARIVGQ
KKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLF
YMTEEGQEGRNAFNQKRQPDFSKFKRNP
>SwissProt__Q8GYN9 1,4-dihydroxy-2-naphthoyl-CoA synthase, peroxisomal; DHNS; Enoyl-CoA hydratase/isomerase D; ECHID; Naphthoate synthase; EC 4.1.3.36 (Arabidopsis thaliana (Mouse-ear cress))
MADSNELGSASRRLSVVTNHLIPIGFSPARADSVELCSASSMDDRFHKVHGEVPTHEVVWKKTDFFGEGDNKEFVDIIYEKALDEGIAKITINRPERRNAFRPQTVKELMRAFNDARDDSSVGVIILTGKGTKAFCSGGDQALRTQDGYADPNDVGRLNVLDLQVQIRRLPKPVIAMVAGYAVGGGHILHMVCDLTIAADNAIFGQTGPKVGSFDAGYGSSIMSRLVGPKKAREMWFMTRFYTASEAEKMGLINTVVPLEDLEKETVKWCREILRNSPTAIRVLKAALNAVDDGHAGLQGLGGDATLLFYGTEEATEGRTAYMHRRPPDFSKFHRRP
>PDB_3h02_A 2.15 angstrom resolution crystal structure of naphthoate synthase from salmonella typhimurium.
DETMLYAPVEWHDCSEGYTDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNVGVIILTGEGDKAFCA
GGDQHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAAENAIFGQTGPKVGSFDGGWGASYMARIVGQKK
AREIWFLCRQYDAQQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYM
TEEGQEGRNAFNQKRQPDFSKFKRNP
>ecocyc__G6715-MONOMER putative ring 1,2-epoxyphenylacetyl-CoA isomerase (oxepin-CoA forming) (EC 5.3.3.18) (Escherichia coli K-12 substr. MG1655)
MMEFILSHVEKGVMTLTLNRPERLNSFNDEMHAQLAECLKQVERDDTIRCLLLTGAGRGFCAGQDLNDRNVDPTGPAPDLGMSVERFYNPLVRRLAKLPKPVICAVNGVAAGAGATLALGGDIVIAARSAKFVMAFSKLGLIPDCGGTWLLPRVAGRARAMGLALLGNQLSAEQAHEWGMIWQVVDDETLADTAQQLARHLATQPTFGLGLIKQAINSAETNTLDTQLDLERDYQRLAGRSADYREGVSAFLAKRSPQFTGK
>ecocyc__NAPHTHOATE-SYN-MONOMER 1,4-dihydroxy-2-naphthoyl-CoA synthase (EC 4.1.3.36) (Escherichia coli K-12 substr. MG1655)
MIYPDEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNIGVIILTGAGDKAFCSGGDQKVRGDYGGYKDDSGVHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDGGWGASYMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMTEEGQEGRNAFNQKRQPDFSKFKRNP
>PDB_3t88_A Crystal structure of escherichia coli menb in complex with substrate analogue, osb-ncoa
DEAMLYAPVEWHDCSEGFEDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNIGVIILTGAGDKAFCS
GGDQKVRGDYGGYKDDSGVHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAADNAIFGQTGPKVGSFDG
GWGASYMARIVGQKKAREIWFLCRQYDAKQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQA
GLQELAGNATMLFYMTEEGQEGRNAFNQKRQPDFSKFKRNP
>biolip__3p85A Crystal structure enoyl-coa hydratase from mycobacterium avium
EILLSNTEERVRTLTLNRPQARNALSAALRDRFFGALADAETDDDVDVVIITGADPVFCAGLDLKELPDISPRWPALTKPVIGAINGAAVTGGLELALYCDILIASENARFADTHARVGLLPTWGLSVRLPQKVGIGLARRMSLTGDYLSAADALRAGLVTEVVPHDQLLGAARAVAASIVGNNQNAVRALLTSYHRIDDAQTSAGLWQEAMAARQFRTSGDDI
>SwissProt__Q7CQ56 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MIYPDETMLYAPVEWHDCSEGYTDIRYEKSTDGIAKITINRPQVRNAFRPLTVKEMIQALADARYDDNVGVIILTGEGDKAFCAGGDQKVRGDYGGYQDDSGVHHLNVLDFQRQIRTCPKPVVAMVAGYSIGGGHVLHMMCDLTIAAENAIFGQTGPKVGSFDGGWGASYMARIVGQKKAREIWFLCRQYDAQQALDMGLVNTVVPLADLEKETVRWCREMLQNSPMALRCLKAALNADCDGQAGLQELAGNATMLFYMTEEGQEGRNAFNQKRQPDFSKFKRNP
>ecocyc__G7516-MONOMER methylmalonyl-CoA decarboxylase (Escherichia coli K-12 substr. MG1655)
MSYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSYDDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELIFTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSEDYQEGMNAFLEKRKPNFVGH
>biolip__2uzfA Crystal structure of staphylococcus aureus 1,4-dihydroxy-2-naphthoyl coa synthase (menb) in complex with acetoacetyl coa
WETLREYDEIKYEFYEGIAKVTINRPEVRNAFTPKTVAEMIDAFSRARDDQNVSVIVLTGEGDLAFCSGGDQKGEDQIPRLNVLDLQRLIRIIPKPVIAMVKGYAVGGGNVLNVVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEKVEDETVQWCKEIMKHSPTALRFLKAAMNADTDGLAGLQQMAGDATLLYYTTDEAKEGRDAFKEKRDPDFDQFPKFP
>PDB_6n97_A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- amino(dethia)-coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>PDB_6n96_A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- oxa(dethia)-coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>PDB_6n95_A Methylmalonyl-coa decarboxylase in complex with 2-sulfonate-propionyl- coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>PDB_6n94_A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- amino(dethia)-coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>PDB_6n93_A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- oxa(dethia)-coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>PDB_6n92_F Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>PDB_6n92_A Methylmalonyl-coa decarboxylase in complex with 2-nitronate-propionyl- coa
AYQYVNVVTINKVAVIEFNYGRKLNALSKVFIDDLMQALSDLNRPEIRCIILRAPSGSKVFSAGHDIHELPSGGRDPLSY
DDPLRQITRMIQKFPKPIISMVEGSVWGGAFEMIMSSDLIIAASTSTFSMTPVNLGVPYNLVGIHNLTRDAGFHIVKELI
FTASPITAQRALAVGILNHVVEVEELEDFTLQMAHHISEKAPLAIAVIKEELRVLGEAHTMNSDEFERIQGMRRAVYDSE
DYQEGMNAFLEKRKPNFVGH
>SwissProt__Q5HH38 1,4-dihydroxy-2-naphthoyl-CoA synthase; DHNA-CoA synthase; EC 4.1.3.36 (Staphylococcus aureus (strain COL))
MTNRQWETLREYDEIKYEFYEGIAKVTINRPEVRNAFTPKTVAEMIDAFSRARDDQNVSVIVLTGEGDLAFCSGGDQKKRGHGGYVGEDQIPRLNVLDLQRLIRIIPKPVIAMVKGYAVGGGNVLNVVCDLTIAADNAIFGQTGPKVGSFDAGYGSGYLARIVGHKKAREIWYLCRQYNAQEALDMGLVNTVVPLEKVEDETVQWCKEIMKHSPTALRFLKAAMNADTDGLAGLQQMAGDATLLYYTTDEAKEGRDAFKEKRDPDFDQFPKFP
>PDB_4eml_A Synechocystis sp. Pcc 6803 1,4-dihydroxy-2-naphthoyl-coenzyme a synthase (menb) in complex with bicarbonate
MDWHIAKHYDDILYYKAGGIAKIVINRPHKRNAFRPQTVFELYDAFCNAREDNRIGVVLLTGAGPHSDGKYAFCSGGDQS
RLNVLDLQRLIRSMPKVVIALVAGYAIGGGHVLHLVCDLTIAADNAIFGQTGPKVGSFDGGFGSSYLARIVGQKKAREIW
YLCRQYSAQEAERMGMVNTVVPVDRLEEEGIQWAKEILSKSPLAIRCLKAAFNADCDGQAGLQELAGNATLLYYMTEEGS
EGKQAFLEKRPPDFSQYPWLP
>PDB_4i52_A Scmenb im complex with 1-hydroxy-2-naphthoyl-coa
MDWHIAKHYDDILYYKAGGIAKIVINRPHKRNAFRPQTVFELYDAFCNAREDNRIGVVLLTGAGPHSDGKYAFCSGGDQS
VRGEGGYIDDQGTPRLNVLDLQRLIRSMPKVVIALVAGYAIGGGHVLHLVCDLTIAADNAIFGQTGPKVGSFDGGFGSSY
LARIVGQKKAREIWYLCRQYSAQEAERMGMVNTVVPVDRLEEEGIQWAKEILSKSPLAIRCLKAAFNADCDGQAGLQELA
GNATLLYYMTEEGSEGKQAFLEKRPPDFSQYPWLP
>metacyc__MONOMER-13896 naphthoyl-CoA synthase (EC 4.1.3.36) (Synechocystis sp. (strain PCC 6803 / Kazusa))
MDWHIAKHYDDILYYKAGGIAKIVINRPHKRNAFRPQTVFELYDAFCNAREDNRIGVVLLTGAGPHSDGKYAFCSGGDQSVRGEGGYIDDQGTPRLNVLDLQRLIRSMPKVVIALVAGYAIGGGHVLHLVCDLTIAADNAIFGQTGPKVGSFDGGFGSSYLARIVGQKKAREIWYLCRQYSAQEAERMGMVNTVVPVDRLEEEGIQWAKEILSKSPLAIRCLKAAFNADCDGQAGLQELAGNATLLYYMTEEGSEGKQAFLEKRPPDFSQYPWLP
>metacyc__HS07490-MONOMER methylglutaconyl-CoA hydratase subunit (EC 4.2.1.18) (Homo sapiens)
MAAAVAAAPGALGSLHAGGARLVAACSAWLCPGLRLPGSLAGRRAGPAIWAQGWVPAAGGPAPKRGYSSEMKTEDELRVRHLEEENRGIVVLGINRAYGKNSLSKNLIKMLSKAVDALKSDKKVRTIIIRSEVPGIFCAGADLKERAKMSSSEVGPFVSKIRAVINDIANLPVPTIAAIDGLALGGGLELALACDIRVAASSAKMGLVETKLAIIPGGGGTQRLPRAIGMSLAKELIFSARVLDGKEAKAVGLISHVLEQNQEGDAAYRKALDLAREFLPQGPVAMRVAKLAINQGMEVDLVTGLAIEEACYAQTIPTKDRLEGLLAFKEKRPPRYKGE
>biolip__3t3wF Crystal structure of probable enoyl-coa hydratase from mycobacterium thermoresistibile
RTEMYIDYDVSDRIATITLNRPEAANAQNPELLDELDAAWTRAAEDNDVSVIVLRANGKHFSAGHDLRGPDKLTLEFIYAHESRRYLEYSLRWRNVPKPSIAAVQGRCISGGLLLCWPCDLIIAAEDALFSDPVVLMDIGGVEYHGHTWELGPRKAKEILFTGRAMTAEEVAQTGMVNRVVPRDRLDAETRALAGEIAKMPPFALRQAKRAVNQTLDVQGFYAAIQSVFDIHQTGHGNAMSVSGWPVL
>SwissProt__O69762 Hydroxycinnamoyl-CoA hydratase-lyase; HCHL; P-hydroxycinnamoyl CoA hydratase/lyase; Trans-feruloyl-CoA hydratase/vanillin synthase; EC 4.1.2.61 (Pseudomonas fluorescens)
MSTYEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPAAGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLLDTEGGREQGMKQFLDDKSIKPGLQAYKR
>biolip__2vssB Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin
YEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPAAGVLVLTGAGEAWTAGMDLKEYFREVDAGPEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTVGHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKLDQSRLLDT
>PDB_2vss_D Wild-type hydroxycinnamoyl-coa hydratase lyase in complex with acetyl- coa and vanillin
TYEGRWKTVKVEIEDGIAFVILNRPEKRNAMSPTLNREMIDVLETLEQDPAAGVLVLTGAGEAWTAGMDLKEYFREVDAG
PEILQEKIRREASQWQWKLLRMYAKPTIAMVNGWCFGGGFSPLVACDLAICADEATFGLSEINWGIPPGNLVSKAMADTV
GHRQSLYYIMTGKTFGGQKAAEMGLVNESVPLAQLREVTIELARNLLEKNPVVLRAAKHGFKRCRELTWEQNEDYLYAKL
DQSRLL
>biolip__3pe8A Crystal structure of enoyl-coa hydratase from mycobacterium smegmatis
SPVLLVDTTDRVRTLTLNRPQSRNALSAELRSTFFRALSDAQNDDDVDVVIVTGADPVFCAGLDLKELSPKWPDMTKPVIGAINGAAVTGGLELALYCDILIASENAKFADTHARVGLMPTWGLSVRLPQKVGVGLARRMSLTGDYLSAQDALRAGLVTEVVAHDDLLTAARRVAASIVGNNQKAVRALLDSYHRIDALQTGGALWAEAEAARQWMRST
>ecocyc__FADB-MONOMER multifunctional enoyl-CoA hydratase, 3-hydroxyacyl-CoA epimerase, Δ3-cis- Δ2-trans-enoyl-CoA isomerase, L-3-hydroxyacyl-CoA dehydrogenase (EC 1.1.1.35; EC 1.1.1.211; EC 4.2.1.17; EC 5.3.3.8; EC 5.1.2.3) (Escherichia coli K-12 substr. MG1655)
MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEPARPVGDLKTA
>biolip__6tnmA E. Coli aerobic trifunctional enzyme subunit-alpha
MLYKGDTLYLDWLEDGIAELVFDAPGSVNKLDTATVASLGEAIGVLEQQSDLKGLLLRSNKAAFIVGADITEFLSLFLVPEEQLSQWLHFANSVFNRLEDLPVPTIAAVNGYALGGGCECVLATDYRLATPDLRIGLPETKLGIMPGFGGSVRMPRMLGADSALEIIAAGKDVGADQALKIGLVDGVVKAEKLVEGAKAVLRQAINGDLDWKAKRQPKLEPLKLSKIEATMSFTIAKGMVAQTAGKHYPAPITAVKTIEAAARFGREEALNLENKSFVPLAHTNEARALVGIFLNDQYVKGKAKKLTKDVETPKQAAVLGAGIMGGGIAYQSAWKGVPVVMKDINDKSLTLGMTEAAKLLNKQLERGKIDGLKLAGVISTIHPTLDYAGFDRVDIVVEAVVENPKVKKAVLAETEQKVRQDTVLASNTSTIPISELANALERPENFCGMHFFNPVHRMPLVEIIRGEKSSDETIAKVVAWASKMGKTPIVVNDCPGFFVNRVLFPYFAGFSQLLRDGADFRKIDKVMEKQFGWPMGPAYLLDVVGIDTAHHAQAVMAAGFPQRMQKDYRDAIDALFDANRFGQKNGLGFWRYKEDSKGKPKKEEDAAVEDLLAEVSQPKRDFSEEEIIARMMIPMVNEVVRCLEEGIIATPAEADMALVYGLGFPPFHGGAFRWLDTLGSAKYLDMAQQYQHLGPLYEVPEGLRNKARHNEPYYPPVEP
>biolip__7xwtB Crystal structure of feruoyl-coa hydratase/lyase complexed with coa from sphingomonas paucimobilis
VEREEDTVRYEIVNNVAWVYYNRPTKRNAQSPKLNRQMLKVLTELEFRDDVGVLVLGGEGPAWCAGMDLKEYFRETEAEGLAGTRKAQREAYTWWERLRWYQKPTIAMVHGWCFGGAYGPLFACDLAFAADEAQFGLSEVNWGILPGGGATKVAVDLMPMRVAMYHAMMGENLSGQDAARYNLVNESMPADQLKARVKQVAETLIQKNWATVKYTKDAVRRVKEMTYDNAEDYLIRLQEGLNWFDKSDGRHVAMKQFLDDKTFKPGLGHYDKTKTEV
>PDB_7xwv_A Feruloyl-coa hydratase/lyase complexed with vanillin and coenzyme a
EREEDTVRYEIVNNVAWVYYNRPTKRNAQSPKLNRQMLKVLTELEFRDDVGVLVLGGEGPAWCAGMDLKEYFRETEAEGL
AGTRKAQREAYTWWERLRWYQKPTIAMVHGWCFGGAYGPLFACDLAFAADEAQFGLSEVNWGILPGGGATKVAVDLMPMR
VAMYHAMMGENLSGQDAARYNLVNESMPADQLKARVKQVAETLIQKNWATVKYTKDAVRRVKEMTYDNAEDYLIRLQEGL
NWFD
>metacyc__HS03720-MONOMER peroxisomal bifunctional enzyme (EC 4.2.1.17; EC 1.1.1.35) (Homo sapiens)
MAEYTRLHNALALIRLRNPPVNAISTTLLRDIKEGLQKAVIDHTIKAIVICGAEGKFSAGADIRGFSAPRTFGLTLGHVVDEIQRNEKPVVAAIQGMAFGGGLELALGCHYRIAHAEAQVGLPEVTLGLLPGARGTQLLPRLTGVPAALDLITSGRRILADEALKLGILDKVVNSDPVEEAIRFAQRVSDQPLESRRLCNKPIQSLPNMDSIFSEALLKMRRQHPGCLAQEACVRAVQAAVQYPYEVGIKKEEELFLYLLQSGQARALQYAFFAERKANKWSTPSGASWKTASARPVSSVGVVGLGTMGRGIVISFARARIPVIAVDSDKNQLATANKMITSVLEKEASKMQQSGHPWSGPKPRLTSSVKELGGVDLVIEAVFEEMSLKKQVFAELSAVCKPEAFLCTNTSALDVDEIASSTDRPHLVIGTHFFSPAHVMKLLEVIPSQYSSPTTIATVMNLSKKIKKIGVVVGNCFGFVGNRMLNPYYNQAYFLLEEGSKPEEVDQVLEEFGFKMGPFRVSDLAGLDVGWKSRKGQGLTGPTLLPGTPARKRGNRRYCPIPDVLCELGRFGQKTGKGWYQYDKPLGRIHKPDPWLSKFLSRYRKTHHIEPRTISQDEILERCLYSLINEAFRILGEGIAASPEHIDVVYLHGYGWPRHKGGPMFYASTVGLPTVLEKLQKYYRQNPDIPQLEPSDYLKKLASQGNPPLKEWQSLAGSPSSKL
>biolip__3omeC Crystal structure of a probable enoyl-coa hydratase from mycobacterium smegmatis
GSMVYIDYGVADSIATITLNRPEAANAQNPELLDELDAAWTRAAEDNEVKVIILRANGKHFSAGHDLRPEKISLEFIIQHEARRYLDYTLRWRNVPKPSIAAVQGRCISGGLLLCWPCDLILASDDALFSDPVALMGIGGVEYHGHTWELGPRKAKEILFTGRALTAEEAERTGMVNRVVARDELDAQTRELAEQIATMPPFALRQAKRAVNQTLDVQGFYAAIQSVFDIHQTGHGNALSVSGWPVL