ID MASZ_MYCBO Reviewed; 741 AA. AC P0A5J5; A0A1R3XZF6; Q50596; X2BIM5; DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 106. 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=BQ2027_MB1868C; OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=233413; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=12788972; DOI=10.1073/pnas.1130426100; RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; RT "The complete genome sequence of Mycobacterium bovis."; RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION. RC STRAIN=ATCC BAA-935 / AF2122/97; RX PubMed=28385856; DOI=10.1128/genomea.00157-17; RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R., RA Robbe-Austerman S., Gordon S.V.; RT "Updated reference genome sequence and annotation of Mycobacterium bovis RT AF2122/97."; RL Genome Announc. 5:E00157-E00157(2017). 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; LT708304; SIU00472.1; -; Genomic_DNA. DR RefSeq; NP_855520.1; NC_002945.3. DR RefSeq; WP_003409271.1; NC_002945.4. DR AlphaFoldDB; P0A5J5; -. DR SMR; P0A5J5; -. DR PATRIC; fig|233413.5.peg.2048; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001419; 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 Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation; KW Reference proteome; Transferase; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250" FT CHAIN 2..741 FT /note="Malate synthase G" FT /id="PRO_0000166890" FT REGION 718..741 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 339 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 633 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 434 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 434 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 459..462 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 462 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 543 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 619 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 741 AA; 80403 MW; A92F54E0FE8B7C64 CRC64; MTDRVSVGNL RIARVLYDFV NNEALPGTDI DPDSFWAGVD KVVADLTPQN QALLNARDEL QAQIDKWHRR RVIEPIDMDA YRQFLTEIGY LLPEPDDFTI TTSGVDAEIT TTAGPQLVVP VLNARFALNA ANARWGSLYD ALYGTDVIPE TDGAEKGPTY NKVRGDKVIA YARKFLDDSV PLSSGSFGDA TGFTVQDGQL VVALPDKSTG LANPGQFAGY TGAAESPTSV LLINHGLHIE ILIDPESQVG TTDRAGVKDV ILESAITTIM DFEDSVAAVD AADKVLGYRN WLGLNKGDLA AAVDKDGTAF LRVLNRDRNY TAPGGGQFTL PGRSLMFVRN VGHLMTNDAI VDTDGSEVFE GIMDALFTGL IAIHGLKASD VNGPLINSRT GSIYIVKPKM HGPAEVAFTC ELFSRVEDVL GLPQNTMKIG IMDEERRTTV NLKACIKAAA DRVVFINTGF LDRTGDEIHT SMEAGPMVRK GTMKSQPWIL AYEDHNVDAG LAAGFSGRAQ VGKGMWTMTE LMADMVETKI AQPRAGASTA WVPSPTAATL HALHYHQVDV AAVQQGLAGK RRATIEQLLT IPLAKELAWA PDEIREEVDN NCQSILGYVV RWVDQGVGCS KVPDIHDVAL MEDRATLRIS SQLLANWLRH GVITSADVRA SLERMAPLVD RQNAGDVAYR PMAPNFDDSI AFLAAQELIL SGAQQPNGYT EPILHRRRRE FKARAAEKPA PSDRAGDDAA R //