ID MASZ_MYCUA Reviewed; 731 AA. AC A0PSI5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 09-JAN-2007, sequence version 1. DT 02-SEP-2026, entry version 107. 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=MUL_3055; OS Mycobacterium ulcerans (strain Agy99). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium; Mycobacterium ulcerans group. OX NCBI_TaxID=362242; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Agy99; RX PubMed=17210928; DOI=10.1101/gr.5942807; RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T., RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J., RA Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M., RA Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.; RT "Reductive evolution and niche adaptation inferred from the genome of RT Mycobacterium ulcerans, the causative agent of Buruli ulcer."; RL Genome Res. 17:192-200(2007). 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=glyoxylate + acetyl-CoA + 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; CP000325; ABL05304.1; -; Genomic_DNA. DR RefSeq; WP_011740916.1; NC_008611.1. DR AlphaFoldDB; A0PSI5; -. DR SMR; A0PSI5; -. DR KEGG; mul:MUL_3055; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_11; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000000765; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-ARBA. DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter. DR GO; GO:0000287; F:magnesium ion binding; IEA:TreeGrafter. DR GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-UniRule. DR GO; GO:0009436; P:glyoxylate catabolic process; IEA:TreeGrafter. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule. DR CDD; cd00728; malate_synt_G; 1. DR FunFam; 3.20.20.360:FF:000002; Malate synthase 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 NCBIfam; NF002825; PRK02999.1; 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 Reference proteome; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..731 FT /note="Malate synthase G" FT /id="PRO_1000056911" FT ACT_SITE 339 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 637 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 118 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 125..126 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 275 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 312 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 339 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 438 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 438 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 463..466 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 466 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 547 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 623 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 731 AA; 79479 MW; BB2A4320CAA7264F CRC64; MTDRVSAGNL RVARVLYDFV NNEALPGTDI DQDSFWAGVD KVVTDLTPQN QDLLKTRDDL QAQIDKWHRH RVIEPLDPQA YREFLTEIGY LLPAPEDFTI TTSGVDDEIT TTAGPQLVVP ILNARFALNA ANARWGSLYD ALYGTDVISE SDGAEKGRGY NKVRGDKVIA YARQFLDDSV PLAGASYTDA TGFKVEDGQL VVSLADTSAA LADPGQFAGY TGTAENPKSI LLANHGLHIE ILIDPESQIG ATDGAGVKDV ILESAITTIM DFEDSVAAVD ADDKALGYRN WLGLNRGDLS EDVTKDDKTF TRVLNTDRTY TAPHGGELTL PGRSLLFVRN VGHLMTNDAI VSDAEGAEGA PVFEGIMDAL FTGLIAIHGL RSTDANGLLT NSRTGSIYIV KPKMHGPAEV AFTCELFSRV EDVLGLPQGT MKVGIMDEER RTTLNLKACI KAAADRVVFI NTGFLDRTGD EIHTSMEAGP MIRKGAMKNT AWIKAYEDAN VDTGLAAGFS GKAQIGKGMW AMTELMADMV EQKIAQPKAG ATTAWVPSPT AATLHAMHYH KVDVFAVQKE LQGKTRTSVD ELLTIPLAKE LAWAPEEIRE EVDNNCQSIL GYVVRWIDQG VGCSKVPDIH NVALMEDRAT LRISSQLLAN WLRHGVITSE DVRASLERMA PLVDKQNAGD PEYHAMAPNF DDSIAFLAAQ DLILSGAQQP NGYTEPILHR RRRELKARAG A //