ID MASZ_PARXL Reviewed; 724 AA. AC Q13YU3; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 22-AUG-2006, sequence version 1. DT 27-MAR-2024, entry version 108. 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=Bxeno_A2208; ORFNames=Bxe_A2223; OS Paraburkholderia xenovorans (strain LB400). OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=266265; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LB400; RX PubMed=17030797; DOI=10.1073/pnas.0606924103; RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L., RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V., RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J., RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T., RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.; RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome RT shaped for versatility."; RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006). 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; CP000270; ABE30746.1; -; Genomic_DNA. DR RefSeq; WP_011488362.1; NZ_CP008760.1. DR AlphaFoldDB; Q13YU3; -. DR SMR; Q13YU3; -. DR STRING; 266265.Bxe_A2223; -. DR KEGG; bxb:DR64_4375; -. DR KEGG; bxe:Bxe_A2223; -. DR PATRIC; fig|266265.5.peg.2309; -. DR eggNOG; COG2225; Bacteria. DR OrthoDB; 9762054at2; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001817; Chromosome 1. 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..724 FT /note="Malate synthase G" FT /id="PRO_1000056900" FT ACT_SITE 340 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 340 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 429 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 429 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 454..457 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 457 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 538 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 724 AA; 79450 MW; 342CB47D2034DB90 CRC64; MTQMNPRGGL QVAANLDQFV ETEALPGTGL DSAAFWSGFD ALVHELAPKN RALLAERDRL QTELDNWHRA NPGPVRDLRA YRAFLEGIGY IVPVPASVKA TTDHVDTEIA EQAGPQLVVP LSNQRYALNA ANARWGSLYD ALYGTDAIPE ANGAEKQKAF NPVRGAAVIA YARRFLDQAA PLANGSHADA TRYGVEGGKL VVTLKNGTSE LKTPAQFIGY QGEESAPSAV LLKHNGLHFE IQIDANDSIG KTDSAHVKDV VVEAAVSTII DCEDSVAAVD ADDKVQLYRN WLGLMNGDLT EEVTKNGKTF TRRLNADRVY TAANGTAPVV LHGRSLLFIR NVGHLMTNPA VLTKDGHEIP EGILDAVITS LCALHDRKHK LNSRTGSIYI VKPKMHGPAE VAFASELFAR VEDLLKLPRN TIKMGIMDEE RRTSVNLLAC INEARERVAF INTGFLDRTG DEMHTAMEAG PMLRKGDMKS SAWIAAYERS NVLVGLSAGL RGRSQIGKGM WAMPDLMHAM LEQKIAHPKA GANTAWVPSP TAATLHALHY HQVDVQAVQQ ELERTDYAKV RDELLDGLLT IPVVAEAKWS DDEIRSEIDN NAQGILGYVV RWIDQGVGCS KVPDIHNVGL MEDRATLRIS SQHIANWLYH GVVKRELVEE TFRRMARVVD EQNAGDPLYK PMAPGFDTIA FKAAQALVFE GRQQPSGYTE PLLHKFRLEV KKEA //