ID MASZ_BRADU Reviewed; 721 AA. AC Q89UE3; DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 30-APR-2003, sequence version 1. DT 27-MAR-2024, entry version 118. 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=bll1474; OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 / OS NBRC 14792 / USDA 110). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Bradyrhizobium. OX NCBI_TaxID=224911; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110; RX PubMed=12597275; DOI=10.1093/dnares/9.6.189; RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.; RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium RT Bradyrhizobium japonicum USDA110."; RL DNA Res. 9:189-197(2002). 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; BA000040; BAC46739.1; -; Genomic_DNA. DR RefSeq; NP_768114.1; NC_004463.1. DR RefSeq; WP_011084290.1; NZ_CP011360.1. DR AlphaFoldDB; Q89UE3; -. DR SMR; Q89UE3; -. DR STRING; 224911.AAV28_04320; -. DR EnsemblBacteria; BAC46739; BAC46739; BAC46739. DR GeneID; 64021353; -. DR KEGG; bja:bll1474; -. DR PATRIC; fig|224911.44.peg.908; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_5; -. DR InParanoid; Q89UE3; -. DR OrthoDB; 9762054at2; -. DR PhylomeDB; Q89UE3; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000002526; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0004474; F:malate synthase activity; IBA:GO_Central. DR GO; GO:0009436; P:glyoxylate catabolic process; IBA:GO_Central. DR GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniRule. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. 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 CHAIN 1..721 FT /note="Malate synthase G" FT /id="PRO_0000166881" FT ACT_SITE 339 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 630 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 117 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 124..125 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 274 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 311 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 431 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 431 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 456..459 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 459 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 540 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 616 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 721 AA; 77928 MW; B34A9EBCEDA1422E CRC64; MKRVDAHGLK IAPVLFDFIA KEAAPKTGIA PDAFWAGVAA IIKDLGPKNR ALLALRDALQ AKIDDWHRAN KGKAFDLNAY TAFLKEIGYL VPEPATQKVE TANVDEEIGK ICGPQLVVPL TNARYALNAA NARWGSLYDA FYGTDAIPHD PSESGKGYNK ARGDKVIAKA KAFLDAAVPL ATGSHTDVTA YSIVAGQLAV KLKSGNATAL KNAAQFAGFQ GDAAAPSAVL LVNNGLHVEV TINRNSAIGK DDPAGVADMV MEAAVSTILD MEDSVAAVDA EDKVLVYRNT LGLMNGTLSA DFEKGGKTLT RSLNADRSYK TPDGKGEVKL HGRSLLLMRN CGHHMFTDAV LDERGEEVPE GLLDAAVSGL LAIHDLKGNS KVKNSRTGSA YIVKPKMHGP DEVSFTCEIF DRVEKMLGLP ENTLKVGIMD EERRTTVNLK ACIQRASKRI MFINTGFLDR TGDEIHTSME AGPMIRKNEM KAQAWIKAYE DWNVDMGLID GLPGHAQIGK GMWAAPDKMA DMLAQKLAHP QAGATTAWVP SPTAATLHAL HYHQVNVIAR QEELTKGGPR AKLSDILTIP VSKSNWAPDD VKQEIDNNCQ GILGYVVRWI DQGVGCSKVP DIHDVGLMED RATLRISSQH LANWLHQGVI TEAQVMESLK RMAVVVDKQN AGDAIYKPMA PAFDGVAFKA ACDLIFKGRE QPNGYTEYIL TARRREAKAA G //