>WP_004513386.1 NCBI__GCF_000012925.1:WP_004513386.1
MSEQISAGKLFRRVIDAEKPLQIVGTINAYCAILAEKAGHRAIYLSGAGVANASFGLPDLGIISRSDVLEEVRRITGASPLPLLVDIDTGWGEEFGIDRTIKEMIRAGAAAVHLEDQVEPKRCGHRPNKSIVSTGRMVDRIKAAVDARSDGDLMIMARTDALATAGLDAAVERAALYVEAGAESIFAEGVTDLAMYRRFADAVDVPLLANMTEFGKTPYYTKEQFAAQGVAMVLYPLSAFRAMSRAALEVYETILRAGTQEPVVAAMQPREELYELLHYYDYERKLDRLSSRDGVESGEGREKR
>ecocyc__G6196-MONOMER 2-methylisocitrate lyase (EC 4.1.3.30) (Escherichia coli K-12 substr. MG1655)
MSLHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCSLPLLVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGAKRCGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDALAVEGLDAAIERAQAYVEAGAEMLFPEAITELAMYRQFADAVQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQYEEKLDNLFARSQVK
>biolip__1mumA Structure of the 2-methylisocitrate lyase (prpb) from escherichia coli
LHSPGKAFRAALTKENPLQIVGTINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCSLPLLVDADIGFGSSAFNVARTVKSMIKAGAAGLHIEDQVGAKRCGHRPNKAIVSKEEMVDRIRAAVDAKTDPDFVIMARTDALAVEGLDAAIERAQAYVEAGAEMLFPEAITELAMYRQFADAVQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEHVYNVLRQEGTQKSVIDTMQTRNELYESINYYQYEEKLDNLFA
>metacyc__MONOMER-13636 2-methylcitrate lyase (EC 4.1.3.30) (Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337))
MTYSASDLARSAGARFRQALADEHPLQVVGTINANHALLAKRAGYRAIYLSGGGVAAGSLGLPDLGISNLDDVLTDIRRITDVCDTPLLVDVDTGFGASAFNVARTTKSLIKFGAAAMHIEDQVGAKRCGHRPNKEIVTQGEMVDRIRAAVDARTDENFVIMARTDALAVEGLDKAIERAVACAEAGADAIFPEAMTDLAMYRKFVDAVKVPVLANITEFGATPLFTTEELGGAGVSMVLYPLSAFRAMNKAAENVYAAIRRDGTQKNVVDTMQTRAELYESIGYHDFEQKLDALFAQGKGK
>reanno__Cup4G11_RR42_RS11260 Methylisocitrate lyase (EC 4.1.3.30) (Cupriavidus basilensis FW507-4G11)
MTFSTSDLARSAGARFRQALADEHPLQVVGTINANHALLAKRAGYRAIYLSGGGVAAGSLGLPDLGISNLDDVLTDVRRITDVCDVPLLVDVDTGFGASAFNVARTTRSLIKFGAGAMHIEDQVGAKRCGHRPGKEIVSQGEMADRIKAAVDARTDENFVIMARTDALAVEGLDKAIERAVACVEAGADAIFPEAMTDLAMYRKFVDAVKVPVLANITEFGATPLFTTEELGGAGVSMVLYPLSAFRAMNKAAENVYAAIRRDGTQQNVVDTMQTRAELYESIGYHAYEQKLDALFAQGKAK
>SwissProt__Q937P0 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 (Cupriavidus necator (Alcaligenes eutrophus) (Ralstonia eutropha))
MTYSASDLARSAGARFRQALADEHPLQVVGTINANHALLAKRAGYRAIYLSGGGVAAGSLGLPDLGISNLDDVLTDIRRITDVCDTPLLVDVDTGFGASAFNVARTTKSLIKFGAAAMHIEDQVGAKRCGHRPNKEIVTQGEMVDRIRAAVDARTDENFVIMARTDALAVEGLDKAIERAVACAEAGADAIFPEAMTDLAMYRKFVDAVKVPVLANITEFGATPLFTTEELDGAGVSMVLLPLSAFRAMNKAAENVYAAIRQDGTQKNVVDTMQTRAELYESIGYHDFEQKLDALFAQGKGK
>SwissProt__Q8EJW1 2-methylisocitrate lyase; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 (Shewanella oneidensis (strain ATCC 700550 / JCM 31522 / CIP 106686 / LMG 19005 / NCIMB 14063 / MR-1))
MTQSAGLRFRQALANSKPLQIVGTTNAYFALMAEQTGFQALYLSGAGVANASYGLPDLGMTSMNDVLIDAGRITSATQLPLLVDIDTGWGGAFNIARTIKEFEKIGVAAVHMEDQVSQKRCGHRPNKAVVSTEEMVDRIKAAVDARTDPNFVIMARTDAVAVEGLEAGIERAKAYIAAGADMIFAEALTELDQYRHFKAQVKAPILANMTEFGQTQLFNKEELAQAGADMVLYPLGTFRAANQAALKVMQALMNDGHQRNVLDTMQTRADLYKYLGYHAFEDKLDQLFSQDK
>metacyc__MONOMER-66 2-methylisocitrate lyase subunit (EC 4.1.3.30) (Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720))
MSLHSPGQAFRAALAKENPLQIVGAINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCPLPLLVDADIGFGSSAFNVARTVKSIAKAGAAALHIEDQVGAKRCGHRPNKAIVSKEEMVDRIRAAVDARTDPNFVIMARTDALAVEGLEAALDRAQAYVDAGADMLFPEAITELSMYRRFADVAQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEKVYTVLRQEGTQKNVIDIMQTRNELYESINYYQFEEKLDALYRNKKS
>reanno__pseudo6_N2E2_Pf6N2E2_6061 Methylisocitrate lyase (EC 4.1.3.30) (Pseudomonas fluorescens FW300-N2E2)
MSNSTPGQRFRDAVANEHPLQVVGTINANHALLAKRAGFKAIYLSGGGVAAGSLGVPDLGITGLDDVLTDVRRITDVCDLPLLVDVDTGFGSSAFNVARTVKSMIKFGAAAIHIEDQVGAKRCGHRPNKEIVSQQEMVDRIKAAVDARTDDSFVIMARTDALAVEGLESALDRAAACIEAGADMIFPEAITELEMYKLFASRVKAPILANITEFGATPLYTTEQLAGADVSLVLYPLSAFRAMNKAAENVYTAIRRDGTQQNVIDTMQTRMELYDRIDYHTFEQKLDALFAAKK
>biolip__6t4vC Crystal structure of 2-methylisocitrate lyase (prpb) from pseudomonas aeruginosa in apo form.
SLTPGQRFREAVATEHPLQVVGTINANHALLAKRAGFKAIYLSGGGVAAGSLGLPDLGISGLDDVLTDVRRITDVCDLPLLVDVDTGFGSSAFNVARTVKSMIKFGAAAMHIEDQVEIVSQQEMVDRIKAAVDARSDDSFVIMARTDALAVEGLQAAIDRACACVEAGADMIFPEAMTELAMYKEFAAAVKVPVLANITEFGATPLFTTDELASADVSLVLYPLSAFRAMNKAAENVYTAIRRDGTQKNVIDTMQTRMELYDRIDYHSFEQKLDALF
>PDB_1o5q_A Crystal structure of pyruvate and mg2+ bound 2-methylisocitrate lyase (prpb) from salmonella typhimurium
SPGQAFRAALAKENPLQIVGAINANHALLAQRAGYQAIYLSGGGVAAGSLGLPDLGISTLDDVLTDIRRITDVCPLPLLV
DADIGFGSSAFNVARTVKSIAKAGAAALHIEDQVAIVSKEEMVDRIRAAVDARTDPNFVIMARTDALAVEGLEAALDRAQ
AYVDAGADMLFPEAITELSMYRRFADVAQVPILANITEFGATPLFTTDELRSAHVAMALYPLSAFRAMNRAAEKVYTVLR
QEGTQKNVIDIMQTRNELYESINYYQFEEKL
>biolip__4iqdA Crystal structure of carboxyvinyl-carboxyphosphonate phosphorylmutase from bacillus anthracis
NKQSTQEELANRFRALVEANEILQIPGAHDAMAALVARNTGFLALYLSGAAYTASKGLPDLGIVTSTEVAERARDLVRATDLPVLVDIDTGFGGVLNVARTAVEMVEAKVAAVQIEDQQLPKKCGHLNGKKLVTTEELVQKIKAIKEVAPSLYIVARTDARGVEGLDEAIERANAYVKAGADAIFPEALQSEEEFRLFNSKVNAPLLANMTEFGKTPYYSAEEFANMGFQMVIYPVTSLRVAAKAYENVFTLIKETGSQKDALSNMQTRSELYETISYHDFEELDTGIAK
>SwissProt__P54528 2-methylisocitrate lyase; 2-MIC; MICL; EC 4.1.3.- (Bacillus subtilis (strain 168))
MSWIVNKQSSQEELAGRFRKLMSAPDILQIPGAHDGMAALLAKEAGFSAIYLSGAAYTASRGLPDLGIITSAEIAERAKDLVRAADLPLLVDIDTGFGGVLNAARTAREMLEARVAAVQMEDQQLPKKCGHLNGKQLVPIKEMAQKIKAIKQAAPSLIVVARTDARAQEGLDAAIKRSEAYIEAGADAIFPEALQAENEFRQFAERIPVPLLANMTEFGKTPYYRADEFEDMGFHMVIYPVTSLRAAAKACERMFGLMKEHGSQKEGLHDMQTRKELYDTISYYDYEALDKTIAKTVLPDE
>SwissProt__Q8NSL2 Probable 2-methylisocitrate lyase 2; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534))
MAGLFSSAVAPTERRKALRAALAAPEIARMPGAFSPLAARAIQEAGFEGVYVSGAVVAADLALPDIGLTTLTEVAHRSRQIARVTDLPVLVDADTGFGEPMSAARTVSELEDAGVAGCHLEDQVNPKRCGHLDGKEVVGTDIMVRRIAAAVNERRDEQFVICARTDAAGVEGIDSAIERAKAYADAGADMIFTEALYSPADFEKFRAAVDIPLLANMTEFGKTELLPAQLLEDIGYNAVIYPVTLLRIAMGQVEQALGDIANTGIQTDWVDRMQHRSRLYELLRYNEYNAFDQQVFTYSADSYKPIF
>metacyc__MONOMER-15044 carboxyphosphonoenolpyruvate phosphonomutase monomer (EC 2.7.8.23) (Streptomyces hygroscopicus)
MAVTKARTFRELMNAPEILVVPSAYDALSAKVIQQAGFPAVHMTGSGTSASMLGLPDLGFTSVSEQAINLKNIVLTVDVPVIMDADAGYGNAMSVWRATREFERVGIVGYHLEDQVNPKRCGHLEGKRLISTEEMTGKIEAAVEAREDEDFTIIARTDARESFGLDEAIRRSREYVAAGADCIFLEAMLDVEEMKRVRDEIDAPLLANMVEGGKTPWLTTKELESIGYNLAIYPLSGWMAAASVLRKLFTELREAGTTQKFWDDMGLKMSFAELFEVFEYSKISELEARFVRDQD
>SwissProt__Q8NSH8 Probable 2-methylisocitrate lyase 1; 2-MIC; MICL; (2R,3S)-2-methylisocitrate lyase; EC 4.1.3.30 (Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534))
MNLFSNGVDVGRRRQAFKAALAAPHIARLPGAFSPLIARSIEEAGFEGVYVSGAVIAADLALPDIGLTTLTEVAHRARQIARVTDLGVLVDADTGFGEPMSAARTVAELEDAGVAGCHLEDQVNPKRCGHLDGKEVVRTDVMVRRIAAAVSARRDPNFVICARTDAAGVEGIDAAIERAKAYLDAGADMIFTEALHSEADFRYFRHAIPDALLLANMTEFGKTTLLSADVLEEIGYNAVIYPVTTLRIAMGQVEQALAEIKEHGTQEGWLDRMQHRSRLYELLRYEDYNVFDQHIFTYRKGENNE
>metacyc__MONOMER-19768 carboxyphosphonoenolpyruvate phosphonomutase (EC 2.7.8.23) (Kitasatospora phosalacinea)
MTTTKARTFRELMNAPEILTVPSAYDALGAKVIEQAGFAAVHMTGSGTSASMLGLPDLGFTSVSEQATNAKNIVLAVDRPVIMDADAGYGNAMNTWRAIREFERAGIVGCHLEDQVNPKRCGHLEGKTLISTEEMCGKIEAAVEARVDPDFTVIARTDARESFGLDEALRRSREYVAAGADCIFLEAMLTVDEMKRVRDELDVPLLANMVEGGKTPWLTTKELEAIGYNLAIYPLSGWMAAASVLQKLYAELRDTGTTQGFWGKYGLGMTFPELFEVFEYGRISELEQRFVRGQD
>BRENDA__Q2L8W6 Methylisocitrate lyase (EC 4.1.3.30) (Toxoplasma gondii)
MTIEFDVPKSFCFDFRKECLEPLSVSTSFFVALPRRLPVLVSAFRLTTSLHSHSMASRAPHAGQRLRSLMQKKCVMLPGAYNGLTARLAAEAGFEGVYVSGAALSACQGVPDIGILGLEDFTRVISQAASVTSLPVLADADTGFGGPEMVRRTVFAYNQAGAAGLHIEDQRLPKKCGHLEGKQLVSIEEMEEKIKAAAAASQDCSNGDFIICARTDARSVDGLDAAVERAVRYTAAGADMLFPEGLETEEEFQAFAHALAVLPGKAPFGGPYLLANMTEFGKTPIMELSTFEGLGYHCVIYPVSPLRVAMKSVKGMLVDLRKNGSVGHSLEKMYTRQELYSTLHYRPEGTWTYPSASVCMDKAVEDTEA
>metacyc__MONOMER-11714 2,3-dimethylmalate lyase subunit (EC 4.1.3.32) (Eubacterium barkeri)
MNTAAKMRELLSTKKMVVAPGAHDAMTAKVIGRLGFDAVYMTGYGQSASHLGQPDVGLLTMTEMVARANAIVEAAGVPVIADADTGFGNAVNVMRTVREYEKAGVAVIQLEDQVMPKKCGHMVGREIVSKEEMVGKIKAAVDTRVNPDFMIMARTDARTTKGIDEALERGLAYKEAGADIIFIESPEGEEEMKRINETIPGYTLANMVEGGRTPLLKNAELEALGYNITIYPTASIYVATKAMVDLWTALKNDDTTAGVMDTMVTFSEFNDLMGLEKIREVEHNYATGR
>SwissProt__Q05957 Petal death protein; (R)-2-methylmalate lyase; D-citramalate lyase; Oxalacetic hydrolase; PSR132; EC 3.7.1.1; EC 4.1.3.- (Dianthus caryophyllus (Carnation) (Clove pink))
MAPPNGTTNGETEVATQGSYTAVSTGRKTTMHRLIEEHGSVLMPGVQDALSAAVVEKTGFHAAFVSGYSVSAAMLGLPDFGLLTTTEVVEATRRITAAAPNLCVVVDGDTGGGGPLNVQRFIRELISAGAKGVFLEDQVWPKKCGHMRGKAVVPAEEHALKIAAAREAIGDSDFFLVARTDARAPHGLEEGIRRANLYKEAGADATFVEAPANVDELKEVSAKTKGLRIANMIEGGKTPLHTPEEFKEMGFHLIAHSLTAVYATARALVNIMKILKEKGTTRDDLDQMATFSEFNELISLESWYEMESKFKNFTPKAT
>biolip__1zlpB Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct
KTTMHRLIEEHGSVLMPGVQDALSAAVVEKTGFHAAFVSGYSVSAAMLGLPDFGLLTTTEVVEATRRITAAAPNLCVVVDGDTGGGGPLNVQRFIRELISAGAKGVFLEDQVWPKKCGHMRGKAVVPAEEHALKIAAAREAIGDSDFFLVARTDARAPHGLEEGIRRANLYKEAGADATFVEAPANVDELKEVSAKTKGLRIANMIEGGKTPLHTPEEFKEMGFHLIAHSLTAVYATARALVNIMKILKEKGTTRDDLDQMATFSEFNELISLESWYEMESKFKN
>PDB_1zlp_A Petal death protein psr132 with cysteine-linked glutaraldehyde forming a thiohemiacetal adduct
KTTMHRLIEEHGSVLMPGVQDALSAAVVEKTGFHAAFVSGYSVSAAMLGLPDFGLLTTTEVVEATRRITAAAPNLCVVVD
GDTGGGGPLNVQRFIRELISAGAKGVFLEDQVWPKKCGHMRGKAVVPAEEHALKIAAAREAIGDSDFFLVARTDARAPHG
LEEGIRRANLYKEAGADATFVEAPANVDELKEVSAKTKGLRIANMIEGGKTPLHTPEEFKEMGFHLIAHSLTAVYATARA
LVNIMKILKEKGTTRDDLDQMATFSEFNELISLESWYEMESKFK
>SwissProt__O49290 Carboxyvinyl-carboxyphosphonate phosphorylmutase, chloroplastic; Carboxyphosphonoenolpyruvate phosphonomutase; CPEP phosphonomutase; EC 2.7.8.23 (Arabidopsis thaliana (Mouse-ear cress))
MSMLMAVKTTSLCCSSLNLTASPTFRRNPRAARLVNPTARIQTRFHRLIEEQGIVLMPGCYDALSAAIVQQTGFSAGFISGYALSASLLGKPDFGLLTPPEMAATARSVCASAPNIPIIADADTGGGNALNIQRTVKDLIAAGAAGCFLEDQAWPKKCGHMRGKQVIPAEEHAAKIASARDAIGDSDFFLVARTDVRATSAKSGLEDAIARVNLYMEAGADASFVEAPRDDDELKEIGKRTKGYRVCNMIEGGVTPLHTPDELKEMGFHLIVHPLTALYASTRALVDVLKTLKENGSTRDHLQKMATFEEFNSLVDLDSWFELEARYSNLRNALGTTKS
>BRENDA__Q2L886 oxaloacetase (EC 3.7.1.1) (Aspergillus niger)
MATAPAVTKLRQLLEDESKIIVCPGVYDGFTARIALQEGFDALYMTGAGTTASRLGQPDLGVVTLNEMRGNAEMIANLDPTVPLIADADTGFGGSLMVHRTVTEYIRAGVAALHLEDQPTSKRCGHLRNKQLVPEDEYLDRIQAAVNARARSHGDIVLIARTDALQSLGYEAAISRLKGAIALGADVAFLEGITSTDQARQVCEELKPTPVLFNNVPGGVSPDLSVQQAQELGFRLIIFPGLALGAVYSAVRGAVQQLKETGTQAVQPGVSPRDLFNVVGLQEAVALDLASGGRLYDKGV
>BRENDA__A2QP68 oxaloacetase (EC 3.7.1.1) (Aspergillus niger)
MPMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTAASVHGQADLGICTLNDMRANAEMISNISPSTPVIADADTGYGGPIMVARTTEQYSRSGVAAFHIEDQVQTKRCGHLAGKILVDTDTYVTRIRAAVQARQRIGSDIVVIARTDSLQTHGYEESVARLRAARDAGADVGFLEGITSREMARQVIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAAMREAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAGGAAFDGGVDLK
>biolip__3fa3B Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form
PMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTAASVHGQADLGICTLNDMRANAEMISNISPSTPVIADADTGYGGPIMVARTTEQYSRSGVAAFHIEDQVQTKRCGHLAGKILVDTDTYVTRIRAAVQARQRIGSDIVVIARTDSLQTHGYEESVARLRAARDAGADVGFLEGITSREMARQVIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAAMREAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAGGAAFDGGVDLK
>metacyc__MONOMER-16188 oxaloacetate acetylhydrolase monomer (EC 3.7.1.1) (Botryotinia fuckeliana)
MPAYSDKVMLTFNNTVKQTTGFESGATKLKNMLRDSNELIVCPGVYDGISARVALQVGFPALYMTGAGTTASRLGMADLGIAQLSDMKDHAEMIANLDPYGPPLIADMDTGYGGPLIIDKAVKSYIRAGVAGFHIEDQIQNKRCGHLQGKKVVPAEEYYMRIRAAKAAKEAMNSDIVLIARTDALQQLGYDECIKRLKVAREMGADVGLLEGYTSKEMAAKTVKEFAPWPILLNMVENGSTPIITTKEAQEMGFRIMIFSFAALAPAYLAIQETFLRLKRDGVVGTPKNLTPKALFDVCGLKDSIVVDTTAGGGAFADGV
>BRENDA__A7ESB3 oxaloacetase (EC 3.7.1.1) (Sclerotinia sclerotiorum)
MAPIMDALPIVEDKPTAAVTDFSVSSPQDGAVVAPPTTVYQTGATKLKNMLRDSNELIVCPGVYDGISTRVALQVGFPALYMTGAGTTASRLGMADLGIAHLSDMKDHAEMIANLDPFGPPLIADMDTGYGGPLIVDKAVKAYIRAGVAGFHIEDQIQNKRCGHLAGKKVVPEEEYYMRIRAAKGAKDAMKSDIVLIARTDALQQLGYDECVKRLKVARELGADVGLLEGYTSKEMAAKTVKEFAPWPILLNMVENGATPIITTKEAQEMGFRIMIFSFAALAPAMLAIQETFVRLKNEGVVGTPKNVTPRALFEVCGLQESIVIDTAAGGGAFADGV
>PDB_3fa3_J Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, trigonal crystal form
MVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTAASVHGQADLGICTLNDMRANAEMISNISPST
PVIADADTGYGGPIMVARTTEQYSRSGVAAFHIEDQVQTKILVDTDTYVTRIRAAVQARQRIGSDIVVIARTDSLQTHGY
EESVARLRAARDAGADVGFLEGITSREMARQVIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAVAA
MREAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAGGAAFDGGVDL
>PDB_3fa4_A Crystal structure of 2,3-dimethylmalate lyase, a pep mutase/isocitrate lyase superfamily member, triclinic crystal form
PMVTAATSLRRALENPDSFIVAPGVYDGLSARVALSAGFDALYMTGAGTAASVHGQADLGICTLNDMRANAEMISNISPS
TPVIADADTGYGGPIMVARTTEQYSRSGVAAFHIEDQVQTGKILVDTDTYVTRIRAAVQARQRIGSDIVVIARTDSLQTH
GYEESVARLRAARDAGADVGFLEGITSREMARQVIQDLAGWPLLLNMVEHGATPSISAAEAKEMGFRIIIFPFAALGPAV
AAMREAMEKLKRDGIPGLDKEMTPQMLFRVCGLDESMKVDAQAG
>BRENDA__Q7Z986 oxaloacetase (EC 3.7.1.1) (Aspergillus niger)
MKVDTPDSASTISMTNTITITVEQDGIYEINGARQEPVVNLNMVTGASKLRKQLRETNELLVCPGVYDGLSARIAINLGFKGMYMTGAGTTASRLGMADLGLAHIYDMKTNAEMIANLDPYGPPLIADMDTGYGGPLMVARSVQQYIQAGVAGFHIEDQIQNKRCGHLAGKRVVTMDEYLTRIRAAKLTKDRLRSDIVLIARTDALQQHGYDECIRRLKAARDLGADVGLLEGFTSKEMARRCVQDLAPWPLLLNMVENGAGPVISVDEAREMGFRIMIFSFACITPAYMGITAALERLKKDGVVGLPEGMGPKKLFEVCGLMDSVRVDTEAGGDGFANGV
>BRENDA__D5LIR7 oxaloacetase (EC 3.7.1.1) (Cryphonectria parasitica)
MASTIAVQEIRLDTTSHSLDRSETPSPIGPLYATGSSSPLKASTTWLQLNSAAPIYVKVQNGSTAAEDEPFSGAKKLRHLLENTDELIVCPGVYDGLSARTAMELGFKSLYMTGAGTTASRLGQPDLAIAQLHDMRDNADMIANLDPFGPPLIADMDTGYGGPIMVARTVEHYIRSGVAGAHLEDQILTKRCGHLSGKKVVSRDEYLVRIRAAVATKRRLRSDFVLIARTDALQSLGYEECIERLRAARDEGADVGLLEGFRSKEQAAAAVAALAPWPLLLNSVENGHSPLITVEEAKAMGFRIMIFSFATLAPAYAAIRETLVRLRDHGVVGTPDGITPVRLFEVCGLQDAMEVDNGAGGKAFSEGV
>biolip__3m0jA Structure of oxaloacetate acetylhydrolase in complex with the inhibitor 3,3-difluorooxalacetate
DEPFSGAKKLRHLLENTDELIVCPGVYDGLSARTAMELGFKSLYMTGAGTTASRLGQPDLAIAQLHDMRDNADMIANLDPFGPPLIADMDTGYGGPIMVARTVEHYIRSGVAGAHLEDQILTKRCGHLSGKKVVSRDEYLVRIRAAVATKRRLRSDFVLIARTDALQSLGYEECIERLRAARDEGADVGLLEGFRSKEQAAAAVAALAPWPLLLNSVENGHSPLITVEEAKAMGFRIMIFSFATLAPAYAAIRETLVRLRDHGVVGTPDGITPVRLFEVCGLQDAMEVDNGAGGKAF