ID A7ZRK3_ECO24 Unreviewed; 723 AA. AC A7ZRK3; DT 23-OCT-2007, integrated into UniProtKB/TrEMBL. DT 23-OCT-2007, sequence version 1. DT 27-MAR-2024, entry version 114. DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; GN Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641, GN ECO:0000313|EMBL:ABV18902.1}; GN OrderedLocusNames=EcE24377A_3435 {ECO:0000313|EMBL:ABV18902.1}; OS Escherichia coli O139:H28 (strain E24377A / ETEC). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=331111 {ECO:0000313|EMBL:ABV18902.1, ECO:0000313|Proteomes:UP000001122}; RN [1] {ECO:0000313|Proteomes:UP000001122} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=E24377A / ETEC {ECO:0000313|Proteomes:UP000001122}; RX PubMed=18676672; DOI=10.1128/JB.00619-08; RA Rasko D.A., Rosovitz M.J., Myers G.S., Mongodin E.F., Fricke W.F., RA Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., RA Henderson I.R., Sperandio V., Ravel J.; RT "The pangenome structure of Escherichia coli: comparative genomic analysis RT of E. coli commensal and pathogenic isolates."; RL J. Bacteriol. 190:6881-6893(2008). CC -!- FUNCTION: Involved in the glycolate utilization. Catalyzes the CC condensation and subsequent hydrolysis of acetyl-coenzyme A (acetyl- CC CoA) and glyoxylate to form malate and CoA. {ECO:0000256|HAMAP- CC Rule:MF_00641}. CC -!- CATALYTIC ACTIVITY: CC Reaction=acetyl-CoA + glyoxylate + H2O = (S)-malate + CoA + H(+); CC Xref=Rhea:RHEA:18181, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:15589, ChEBI:CHEBI:36655, ChEBI:CHEBI:57287, CC ChEBI:CHEBI:57288; EC=2.3.3.9; CC Evidence={ECO:0000256|ARBA:ARBA00001699, ECO:0000256|HAMAP- CC Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, ECO:0000256|HAMAP- CC Rule:MF_00641}; CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from CC isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641, CC ECO:0000256|RuleBase:RU003572}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641, CC ECO:0000256|RuleBase:RU003572}. CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000800; ABV18902.1; -; Genomic_DNA. DR RefSeq; WP_000084091.1; NC_009801.1. DR AlphaFoldDB; A7ZRK3; -. DR KEGG; ecw:EcE24377A_3435; -. DR HOGENOM; CLU_028446_1_0_6; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001122; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR CDD; cd00728; malate_synt_G; 1. DR Gene3D; 3.20.20.360; Malate synthase, domain 3; 2. DR Gene3D; 1.20.1220.12; Malate synthase, domain III; 1. DR HAMAP; MF_00641; Malate_synth_G; 1. DR InterPro; IPR044856; Malate_synth_C_sf. DR InterPro; IPR011076; Malate_synth_sf. DR InterPro; IPR001465; Malate_synthase_TIM. DR InterPro; IPR006253; Malate_synthG. DR InterPro; IPR048355; MS_C. DR InterPro; IPR048356; MS_N. DR InterPro; IPR046363; MS_N_TIM-barrel_dom. DR InterPro; IPR048357; MSG_insertion. DR NCBIfam; TIGR01345; malate_syn_G; 1. DR PANTHER; PTHR42739; MALATE SYNTHASE G; 1. DR PANTHER; PTHR42739:SF1; MALATE SYNTHASE G; 1. DR Pfam; PF20659; MS_C; 1. DR Pfam; PF20656; MS_N; 1. DR Pfam; PF01274; MS_TIM-barrel; 1. DR Pfam; PF20658; MSG_insertion; 1. DR SUPFAM; SSF51645; Malate synthase G; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:ABV18902.1}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641}; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641}; KW Reference proteome {ECO:0000313|Proteomes:UP000001122}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00641}. FT DOMAIN 16..77 FT /note="Malate synthase N-terminal" FT /evidence="ECO:0000259|Pfam:PF20656" FT DOMAIN 158..233 FT /note="Malate synthase G alpha-beta insertion" FT /evidence="ECO:0000259|Pfam:PF20658" FT DOMAIN 335..579 FT /note="Malate synthase TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01274" FT DOMAIN 591..695 FT /note="Malate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF20659" FT ACT_SITE 338 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT ACT_SITE 631 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT BINDING 118 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 125..126 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 274 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 311 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 338 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 427 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 427 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 452..455 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 455 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 536 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT MOD_RES 617 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT MOD_RES 688 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" SQ SEQUENCE 723 AA; 80519 MW; 4B160E959727C3F2 CRC64; MSQTITQGRL RIDANFKRFV DEEVLPGTGQ DAAAFWRNFD EIVHDLAPEN RQLLAERDRI QAALDEWHRS NPGPVKDKAA YKSFLRELGY LVPQPERVTV ETTGIDSEIT SQAGPQLVVP AMNARYALNA ANARWGSLYD ALYGSDIIPQ EGAMVSGYDP QRGEQVIAWV RRFLDESLPL ENGSYQDVVA FKVVDKQLRI QLKNGKETTL RTPAQFVGYR GDAAALTCIL LKNNGLHIEL QIDANGRIGK DDPAHINDVI VEAAISTILD CEDSVAAVDA EDKILLYRNL LGLMQGTLQE KMEKNGRQIV RKLNDDRHYT AADGSEISLH GRSLLFIRNV GHLMTIPVIW DSEGNEIPEG ILDGVMTGAI ALYDLKVQKN SRTGSVYIVK PKMHGPQEVA FANKLFTRIE TMLGMAPNTL KMGIMDEERR TSLNLRSCIA QARNRVAFIN TGFLDRTGDE MHSVMEAGPM LRKNQMKSTP WIKAYERNNV LSGLFCGLRG KAQIGKGMWA MPDLMADMYS QKGDQLRAGA NTAWVPSPTA ATLHALHYHQ TNVQSVQANI AQTEFNAEFE PLLDDLLTIP VAENANWSVE EIQQELDNNV QGILGYVVRW VEQGIGCSKV PDIHNVALME DRATLRISSQ HIANWLRHGI LTKEQVQASL ENMAKVVDQQ NAGDPAYRPM AGNFANSCAF KAASDLIFLG VKQPNGYTEP LLHAWRLREK ESH //