ID MASZ_MYCSS Reviewed; 731 AA. AC Q1B860; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2006, sequence version 1. DT 27-MAR-2024, entry version 102. 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=Mmcs_2817; OS Mycobacterium sp. (strain MCS). OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae; OC Mycobacterium. OX NCBI_TaxID=164756; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=MCS; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., RA Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.; RT "Complete sequence of chromosome of Mycobacterium sp. MCS."; RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases. 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; CP000384; ABG08924.1; -; Genomic_DNA. DR AlphaFoldDB; Q1B860; -. DR SMR; Q1B860; -. DR KEGG; mmc:Mmcs_2817; -. DR HOGENOM; CLU_028446_1_0_11; -. DR BioCyc; MSP164756:G1G6O-2871-MONOMER; -. DR UniPathway; UPA00703; UER00720. 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..731 FT /note="Malate synthase G" FT /id="PRO_1000056909" FT ACT_SITE 342 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 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 277 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 314 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 342 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 731 AA; 79921 MW; 05AB383646FED936 CRC64; MTDRVTVGNL RVARALYDFI TDEALAGTDL DPDSFWSGVD KVVADLTPRN QELLARRDDL QAQIDKWHRQ RAIGPHDADE YKQFLTEIGY LEPDPGDFTI TTAGVDDEIT TTAGPQLVVP VLNARFALNA ANARWGSLYD ALYGTDVISE EDGAEKGTSY NRVRGDKVIA YAREFLDGAA PLASGSYADA TGFRIEDGQV QVELGDDQWV GLADPDQFVG YTGELGSPQW SILLRNNGLH IEILIDPDSP VGSTDKAGVK DVVLESAVTT IMDFEDSVAA VDAEDKVLGY RNWLGLNRGD LSEEVSKGDK TFTRVLNPDR TYTTPDGSGE LTLPGRSLLF VRNVGHLMTN DAITDAEGNE VFEGIQDALF TGLIAMHGLK ESDANGPLRN SRTGSVYIVK PKMHGPAEVA YTVDLFSRVE DVLGLPQNTL KVGIMDEERR TTLNLKACIK AAADRVVFIN TGFLDRTGDE IHTSMEAGPM IRKGAMKSQP WIKAYEDQNV DVGLATGFSG RAQIGKGMWA MTDLMADMVE QKIGQPKAGA TTAWVPSPTA ATLHAMHYHQ VDVYAVHKEL EGKQRASLDD LLTIPLAKEL AWAPEEIREE VDNNCQSILG YVVRWIDAGV GCSKVPDIHD IALMEDRATL RISSQLLANW LRHGVITEED VKTSLRRMAA VVDEQNAKDP DFKPMATDPD SSIAFQAAQE LILAGGTQPS GYTEPILHRR RREYKASVAG A //