>WP_108402814.1 NCBI__GCF_003063475.1:WP_108402814.1
MNLPRRVKLIDVGPRDGLQNEKQPVPAAVKVELVHRLQDAGLNEIEVTSFVSPKWVPQMADNAEVMAGIHRQPDVRYSVLTPNLQGFEAALKTKPDEIVVFGAASEAFSQKNINCSIEESIERFAPVVKAARDAGIAVRGAMSCTVGCPYEGEIAPERVGYLAGLMKSIGIQRVDVADTIGVGTPRKVQAAIEATLRHYALNDVSGHFHDTYGQALVNTLAALQVGVWNFQSSVAGLGGCPYAKGATGNVATEDVVYMLQGMGIETGIHLDKLIDAGVFISNALGRQPNSLVSRAVLNKRAV
>metacyc__HS04116-MONOMER Hydroxymethylglutaryl-CoA lyase, mitochondrial (EC 4.1.3.4) (Homo sapiens)
MAAMRKALPRRLVGLASLRAVSTSSMGTLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATCKL
>biolip__2cw6A Crystal structure of human hmg-coa lyase: insights into catalysis and the molecular basis for hydroxymethylglutaric aciduria
TLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLTPNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAEVTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCPYAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATC
>PDB_3mp3_B Crystal structure of human lyase in complex with inhibitor hg-coa
TLPKRVKIVEVGPRDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLT
PNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAE
VTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCP
YAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATC
>SwissProt__P97519 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 (Rattus norvegicus (Rat))
MATVRKAFPQRLVGLASLRAASTSSMGTLPKRVKIVEVGPRDGLQNEKSIVPTPVKIKLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSIFGAASELFTRKNVNCSIEESFQRFDGVMQAARAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVLHEVPVAALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLTGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL
>PDB_3mp5_B Crystal structure of human lyase r41m in complex with hmg-coa
TLPKRVKIVEVGPMDGLQNEKNIVSTPVKIKLIDMLSEAGLSVIETTSFVSPKWVPQMGDHTEVLKGIQKFPGINYPVLT
PNLKGFEAAVAAGAKEVVIFGAASELFTKKNINCSIEESFQRFDAILKAAQSANISVRGYVSCALGCPYEGKISPAKVAE
VTKKFYSMGCYEISLGDTIGVGTPGIMKDMLSAVMQEVPLAALAVHCHDTYGQALANTLMALQMGVSVVDSSVAGLGGCP
YAQGASGNLATEDLVYMLEGLGIHTGVNLQKLLEAGNFICQALNRKTSSKVAQATC
>SwissProt__P38060 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 (Mus musculus (Mouse))
MASVRKAFPRRLVGLTSLRAVSTSSMGTLPKQVKIVEVGPRDGLQNEKSIVPTPVKIRLIDMLSEAGLPVIEATSFVSPKWVPQMADHSDVLKGIQKFPGINYPVLTPNMKGFEEAVAAGAKEVSVFGAVSELFTRKNANCSIEESFQRFAGVMQAAQAASISVRGYVSCALGCPYEGKVSPAKVAEVAKKLYSMGCYEISLGDTIGVGTPGLMKDMLTAVMHEVPVTALAVHCHDTYGQALANTLVALQMGVSVVDSSVAGLGGCPYAKGASGNLATEDLVYMLNGLGIHTGVNLQKLLEAGDFICQALNRKTSSKVAQATCKL
>SwissProt__D4A5C3 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; EC 4.1.3.4 (Rattus norvegicus (Rat))
MGNLPSAAKHCLNYQQLLREHLWSGESVAGALDPAQEASQLSGLPEYVKIVEVGPRDGLQNEKVIVPTDIKIEFINQLSQTGLSVIEVTSFVSSRWVPQMADHAEVMGGIHQYPGVRYPVLVPNLQGLQHAVAAGATEIAVFGAASESFSKKNINCSIEESMGRFEQVISSARHMNIPVRGYVSCALGCPYEGSIMPQKVTEVSKRLYSMGCYEISLGDTVGVGTPGSMKTMLESVMKEIPPGALAVHCHDTYGQALANILTALQMGINVVDSAVSGLGGCPYAKGASGNVATEDLIYMLNGMGLNTGVDLHKVMEAGDFICKAVNKTTNSKVAQASFKARLE
>SwissProt__Q8TB92 3-hydroxy-3-methylglutaryl-CoA lyase, cytoplasmic; 3-hydroxy-3-methylglutaryl-CoA lyase-like protein 1; HMGCL-like 1; Endoplasmic reticulum 3-hydroxy-3-methylglutaryl-CoA lyase; er-cHL; EC 4.1.3.4 (Homo sapiens (Human))
MGNVPSAVKHCLSYQQLLREHLWIGDSVAGALDPAQTSLLTNLHCFQPDVSGFSVSLAGTVACIHWETSQLSGLPEFVKIVEVGPRDGLQNEKVIVPTDIKIEFINRLSQTGLSVIEVTSFVSSRWVPQMADHTEVMKGIHQYPGVRYPVLTPNLQGFHHAVAAGATEISVFGAASESFSKKNINCSIEESMGKFEEVVKSARHMNIPARGYVSCALGCPYEGSITPQKVTEVSKRLYGMGCYEISLGDTIGVGTPGSMKRMLESVMKEIPPGALAVHCHDTYGQALANILTALQMGINVVDSAVSGLGGCPYAKGASGNVATEDLIYMLNGLGLNTGVNLYKVMEAGDFICKAVNKTTNSKVAQASFNA
>metacyc__MONOMER-16069 hydroxymethylglutaryl-CoA lyase subunit (EC 4.1.3.26; EC 4.1.3.4) (Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1))
MNLPKKVRLVEVGPRDGLQNEKQPIEVADKIRLVDDLSAAGLDYIEVGSFVSPKWVPQMAGSAEVFAGIRQRPGVTYAALAPNLKGFEAALESGVKEVAVFAAASEAFSQRNINCSIKDSLERFVPVLEAARQHQVRVRGYISCVLGCPYDGDVDPRQVAWVARELQQMGCYEVSLGDTIGVGTAGATRRLIEAVASEVPRERLAGHFHDTYGQALANIYASLLEGIAVFDSSVAGLGGCPYAKGATGNVASEDVLYLLNGLEIHTGVDMHALVDAGQRICAVLGKSNGSRAAKALLAKA
>SwissProt__O81027 Hydroxymethylglutaryl-CoA lyase, mitochondrial; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 (Arabidopsis thaliana (Mouse-ear cress))
MQWNGVRRAHSIWCKRLTNNTHLHHPSIPVSHFFTMSSLEEPLSFDKLPSMSTMDRIQRFSSGACRPRDDVGMGHRWIEGRDCTTSNSCIDDDKSFAKESFPWRRHTRKLSEGEHMFRNISFAGRTSTVSGTLRESKSFKEQKYSTFSNENGTSHISNKISKGIPKFVKIVEVGPRDGLQNEKNIVPTSVKVELIQRLVSSGLPVVEATSFVSPKWVPQLADAKDVMDAVNTLDGARLPVLTPNLKGFQAAVSAGAKEVAIFASASESFSLSNINCTIEESLLRYRVVATAAKEHSVPVRGYVSCVVGCPVEGPVLPSKVAYVVKELYDMGCFEISLGDTIGIGTPGSVVPMLEAVMAVVPADKLAVHFHDTYGQALANILVSLQMGISIVDSSIAGLGGCPYAKGASGNVATEDVVYMLNGLGVHTNVDLGKLIAAGDFISKHLGRPNGSKAAVALNRRITADASKI
>biolip__1ydnA Crystal structure of the hmg-coa lyase from brucella melitensis, northeast structural genomics target lr35.
AEHVEIVEMAARDGLQNEKRFVPTADKIALINRLSDCGYARIEATSFVSPKWVPQLADSREVMAGIRRADGVRYSVLVPNMKGYEAAAAAHADEIAVFISASEGFSKANINCTIAESIERLSPVIGAAINDGLAIRGYVSCVVECPYDGPVTPQAVASVTEQLFSLGCHEVSLGDTIGRGTPDTVAAMLDAVLAIAPAHSLAGHYHDTGGRALDNIRVSLEKGLRVFDASVGGLGGCPFAPGAKGNVDTVAVVEMLHEMGFETGLDLDRLRSAGLFTQALRQD
>reanno__Smeli_SM_b21125 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) (Sinorhizobium meliloti 1021)
MTSPAKERVTIVEVAPRDGLQNESRLVATEDKIRLVDLLADCGYERIEVTSFVSPRWVPQLADAPAVMAGIVRRPGTRYAALTPNMRGFEAALAAGADEVAIFASASESFSERNINCSIAESIERFRPVAEASRHRGVPLRGYVSCVVECPYEGAIVPAETARVARLLADLGCYEISLGDTIGRGTPEAVDAMLAAALREIDAPKLAGHFHDTSGRALENIAVALERGIRVFDASAGGLGGCPYAPGAAGNVDTLAVNAFLEAQSFATGLDSEKLDRAAAFARSLRSTA
>metacyc__MONOMER-11828 hydroxymethylglutaryl-CoA lyase monomer (EC 4.1.3.4) (Pseudomonas mevalonii)
MQAVKVFEVGPRDGLQNERQPLSVAARVGLIGELAGTGLRHIEAGAFVSPRWVPQMAGSDEVLRQLPSNDGVSYTALVPNRQGFEAAQRAGCREVAVFAAASEAFSRNNINCSIDESFERFTPVLRAANEASIRVRGYVSCVLGCPFSGAVAPEAVAKVARRLYELGCYEISLGDTIGAGRPDETAQLFELCARQLPVAALAGHFHDTWGMAIANVHAALAQGVRTFDSSVAGLGGCPYSPGASGNVATEDLLYLLHGLGYSTGVDLEAVAQVGVRISAQLGTANRSRAGLALAARSAREH
>SwissProt_P13703 Hydroxymethylglutaryl-CoA lyase; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 from Pseudomonas mevalonii
MQAVKVFEVGPRDGLQNERQPLSVAARVGLIGELAGTGLRHIEAGAFVSPRWVPQMAGSDEVLRQLPSNDGVSYTALVPN
RQGFEAAQRAGCREVAVFAAASEAFSRNNINCSIDESFERFTPVLRAANEASIRVRGYVSCVLGCPFSGAVAPEAVAKVA
RRLYELGCYEISLGDTIGAGRPDETAQLFELCARQLPVAALAGHFHDTWGMAIANVHAALAQGVRTFDSSVAGLGGCPYS
PGASGNVATEDLLYLLHGLGYSTGVDLEAVAQVGVRISAQLGTANRSRAGLALAARSAREH
>CharProtDB__CH_122457 3-hydroxy-3-methylglutaryl-coenzyme A lyase/3-methylglutaconyl-coenzyme A hydratase; EC 4.1.3.4; EC 4.2.1.18 (Emericella nidulans)
MQNSTKTVRIVEVGPRDGLQNIPQSIDSTIKLDLIRRLRDAGLQTIELTSFVSPRAIPQLADAQVVVQNADIQKLLKNPKLRLPVLVPNLKGLERALHNGIKEVAVFISATEGFSRANINCTVDEGLERARQVASRAASAGLSVRGYVSCIFADPYDGPTRPSSVLRCTKALLDAGCYEVSLGDTLGIGTPADVRWLITYLQDNGVPLEMLAGHFHDTYGGAVANVWEAYKCGLRMFDSSVAGLGGCPXALGAKGNVASEDLVYMFERSGIHTGVDLSKLVETGEWISRQLSIAISSRAGAALWAMRKQTAVPKSPKVSVSWKLVKQTEGLQLFRSGVNLRINLNRPKNGNALTAIMAQDLTEAVTNAGRDATISRIILTGSGKFFCTGMDLGKGSTAVGQGGSSSNAQFDRLTNLFEAIDQSPKVTIACLNGPAFGGGVGLAFACDMRFAVRAASVTLSEVKLGLCPATISKYVIREFGIALSREAMLSARPVSAGELKARGLVVELADNAEALPGLLDQFLTQLKAASPEASRMSKELIRLAWAHGGKEEQAKGIRALFDGMMRPDGDGAHGVKEFQAKRSVDWDAYTLRRVDSAKV
>SwissProt__O34873 Hydroxymethylglutaryl-CoA lyase YngG; HL; HMG-CoA lyase; 3-hydroxy-3-methylglutarate-CoA lyase; EC 4.1.3.4 (Bacillus subtilis (strain 168))
MPYPKKVTIKEVGPRDGLQNEPVWIATEDKITWINQLSRTGLSYIEITSFVHPKWIPALRDAIDVAKGIDREKGVTYAALVPNQRGLENALEGGINEACVFMSASETHNRKNINKSTSESLHILKQVNNDAQKANLTTRAYLSTVFGCPYEKDVPIEQVIRLSEALFEFGISELSLGDTIGAANPAQVETVLEALLARFPANQIALHFHDTRGTALANMVTALQMGITVFDGSAGGLGGCPYAPGSSGNAATEDIVYMLEQMDIKTNVKLEKLLSAAKWIEEKMGKPLPSRNLQVFKSS
>biolip__6ndsA Structure of an hmg-coa lyase from acenitobacter baumannii in complex with coenzyme a and 3-methylmalate
MTAFSDLLVVQEVSPRDGLQIEPTWVPTDKKIDLINQLSTMGFSRIEAGSFVSPKAIPNLRDGEEVFTGITRHKDIIYVGLIPNLKGALRAVEANANELNLVLSASQTHNLANMRMTKAQSFAGFTEIVEQLQGKTQFNGTVATTFGCPFEGKISEREVFSLVEHYLKLGIHNITLADTTGMANPVQVKRIVSHVLSLISPEQLTLHFHNTRGLGLTNVLAAYEVGARRFDAALGGLGGCPFAPGASGNICTEDLVNMCEEIGIPTTIDLDALIQLSRTLPALLGHDTPSQLAKAGRNTDLHPIP
>SwissProt__A9WGE2 (R)-citramalyl-CoA lyase; EC 4.1.3.46 (Chloroflexus aurantiacus (strain ATCC 29366 / DSM 635 / J-10-fl))
MEAVTIVDVAPRDGLQNEPDVLEPATRVELIERLLAAGVPRIEIGSFVNPRQVPQMAGIDQIARMLIERGHNLAARTTNDLFRFTALVPNQRGYELAAAAGLRHVRLVLAASDGLNRANFKRTTAESLIEFSRFALNIRRDGLTFGVAIGAAFGCPFDGYVSPERVRAIAEHAVDIGAGEIILADTTGMAVPTQVAALCRTILDRIPDVTVTLHLHNTRNTGYANAFAAWQVGIRSFDAALGGIGGCPFAPRAVGNIASEDLVHLFNGLGVPTGIDLSALIAASDWLSATLGRPLPALVGKAGPVYPQVVSMAPYLS
>reanno__Pedo557_CA265_RS13115 Hydroxymethylglutaryl-CoA lyase (EC 4.1.3.4) (Pedobacter sp. GW460-11-11-14-LB5)
MSQNNFKLVECPRDAMQGLHDFVPTKLKAEYLNLLLQVGFDTLDFGSFVSPKAIPQMADTAEVLAQLDLSNTSTKLLAIVANLRGVEDAVKHQAVNYLGFPFSISETFQQRNTNSSIAQSLNTVEEMLSLCAKNNKKAVVYLSMGFGNPYGDKWNYEIVEKWADVLVSRGVEILSLADTVGISTPEKIENILPKLISRFSNTEIGIHLHSTPAERFEKIEAAYHSGVKRIDSALKGFGGCPMAADDLTGNIATEDVITFLNMKGEKLNLNMDKWNEAMVLSGKIFG