ID MASZ_BRUO2 Reviewed; 728 AA. AC A5VS09; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 27-MAR-2024, entry version 89. DE RecName: Full=Malate synthase G {ECO:0000255|HAMAP-Rule:MF_00641}; DE EC=2.3.3.9 {ECO:0000255|HAMAP-Rule:MF_00641}; GN Name=glcB {ECO:0000255|HAMAP-Rule:MF_00641}; GN OrderedLocusNames=BOV_1595; OS Brucella ovis (strain ATCC 25840 / 63/290 / NCTC 10512). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Brucellaceae; Brucella/Ochrobactrum group; Brucella. OX NCBI_TaxID=444178; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25840 / 63/290 / NCTC 10512; RX PubMed=19436743; DOI=10.1371/journal.pone.0005519; RA Tsolis R.M., Seshadri R., Santos R.L., Sangari F.J., Lobo J.M., RA de Jong M.F., Ren Q., Myers G., Brinkac L.M., Nelson W.C., Deboy R.T., RA Angiuoli S., Khouri H., Dimitrov G., Robinson J.R., Mulligan S., RA Walker R.L., Elzer P.E., Hassan K.A., Paulsen I.T.; RT "Genome degradation in Brucella ovis corresponds with narrowing of its host RT range and tissue tropism."; RL PLoS ONE 4:E5519-E5519(2009). 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:0000255|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; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00641}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00641}; CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from CC isocitrate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00641}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00641}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00641}. CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00641}. 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; CP000708; ABQ60552.1; -; Genomic_DNA. DR RefSeq; WP_006155575.1; NC_009505.1. DR AlphaFoldDB; A5VS09; -. DR SMR; A5VS09; -. DR GeneID; 45124960; -. DR KEGG; bov:BOV_1595; -. DR HOGENOM; CLU_028446_1_0_5; -. DR PhylomeDB; A5VS09; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000006383; Chromosome I. 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 Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation; KW Transferase; Tricarboxylic acid cycle. FT CHAIN 1..728 FT /note="Malate synthase G" FT /id="PRO_1000056899" FT ACT_SITE 345 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 636 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 123 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 130..131 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 281 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 318 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 345 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 437 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 437 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 462..465 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 465 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 546 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 622 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 728 AA; 80030 MW; 2582CF1496CEFF00 CRC64; MGSAEKRNYV EIEGLAVAPE LVEFLAKEAA PGTGVEPEKF WKGFATIIRD LAPKNRALLA KRDELQARID AWYKENRDKG YSQADYQQFL KDIGYLLPEG GAFSVSTTNV DPEITHIAGP QLVVPVMNAR YALNAANARW GSLYDALYGT DAISEADGAE KGKGYNPKRG EKVIAWAKNF LDESAPLSTG KWADVAGLAV NDGKLEIRLT DGSATTLKDE SQFNGYNGDA ASPTNVLLAK HNMHVDIVIN ADHPIGKTDP AHIADVVLES AISTIQDCED SIAAVDAEDK VAVYRNWLGL MNGKLEDTFE KNGKQMTRRL NGDRTYTAPD GSTLTLKGRS LMLVRNVGHL MTNPAILDAE GNEVPEGIMD AAFTSLIALH DIGPNGRHMN SREGSVYIVK PKMHGPEEVA FANEIFTRTE EMLGMKPNTL KIGIMDEERR TTVNLKEAIR AAKDRVVFIN TGFLDRTGDE IHTSMEAGPM IRKGDMKQAA WIGAYEQWNV DIGLECGLSG HAQIGKGMWA MPDMMAAMLE QKIAHPKAGA NTAWVPSPTA ATLHATHYHK IDVVAVQEKL KSRPRAKLDD ILSVPVAVRP NWTPDDIQHE IDNNAQGILG YVVRWIDQGV GCSKVPDINN VGLMEDRATL RISAQHIANW LYHGVVSEAQ VMETMKRMAA IVDKQNEGDP LYRPMAADFD KSIAFQAACD LVFKGREQPN GYTEPVLHRR RLELKQAS //