ID MASZ_PSEF5 Reviewed; 725 AA. AC Q4K4S5; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 02-AUG-2005, 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=PFL_5700; OS Pseudomonas fluorescens (strain ATCC BAA-477 / NRRL B-23932 / Pf-5). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=220664; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-477 / NRRL B-23932 / Pf-5; RX PubMed=15980861; DOI=10.1038/nbt1110; RA Paulsen I.T., Press C.M., Ravel J., Kobayashi D.Y., Myers G.S.A., RA Mavrodi D.V., DeBoy R.T., Seshadri R., Ren Q., Madupu R., Dodson R.J., RA Durkin A.S., Brinkac L.M., Daugherty S.C., Sullivan S.A., Rosovitz M.J., RA Gwinn M.L., Zhou L., Schneider D.J., Cartinhour S.W., Nelson W.C., RA Weidman J., Watkins K., Tran K., Khouri H., Pierson E.A., Pierson L.S. III, RA Thomashow L.S., Loper J.E.; RT "Complete genome sequence of the plant commensal Pseudomonas fluorescens RT Pf-5."; RL Nat. Biotechnol. 23:873-878(2005). 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; CP000076; AAY94890.1; -; Genomic_DNA. DR RefSeq; WP_011063875.1; NC_004129.6. DR AlphaFoldDB; Q4K4S5; -. DR SMR; Q4K4S5; -. DR STRING; 220664.PFL_5700; -. DR GeneID; 57478650; -. DR KEGG; pfl:PFL_5700; -. DR PATRIC; fig|220664.5.peg.5811; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_6; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000008540; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004474; F:malate synthase activity; ISS:JCVI. 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; ISS:JCVI. 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..725 FT /note="Malate synthase G" FT /id="PRO_1000056919" FT ACT_SITE 340 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 631 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 276 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 313 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 432 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 432 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 457..460 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 460 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 541 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT MOD_RES 617 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 725 AA; 78859 MW; 85D274924CF2CD44 CRC64; MTEHVQVGGL QVARVLFDFV NNEAIPGTGL TADSFWAGAD KVIHDLAPKN KALLAKRDDF QARIDAWHQS RAGQAHDAVA YKAFLQDIGY LLPEAADFQA TTQNVDEEIA HMAGPQLVVP VMNARFALNA SNARWGSLYD ALYGTDAISE ADGAEKGKGY NKVRGDKVIA FARAFLDESA PLTAGSHVDS VSYKIVGGKL VVGLKGGSNS GLRNDAQLIG YQGDAAAPTA ILLKHNGLHF EIQIDATSPV GQTDAAGVKD LLMEAALTTI MDCEDSVAAV DADDKVVIYR NWLGLMKGDL AEEVSKGGKS FTRTMNADRE YTGVNGEPVK LHGRSLLFVR NVGHLMTIDA ILDKDGNEVP EGILDGLVTS LASIHNLNGN TSRKNSRTGS MYIVKPKMHG PEEAAFTNEL FGRIEEVLNL PRNTLKVGIM DEERRTTVNL KACIKAASER VVFINTGFLD RTGDEIHTSM EAGAMVRKAD MKAEKWIGAY ENWNVDIGLS TGLQGRAQIG KGMWAMPDLM AAMLEQKIAH PLAGANTAWV PSPTAAALHA LHYHKVDVFA RQAELAKRAR ASVDDILTIP LAVNPSWTPE QIKNELDNNA QGILGYVVRW IDQGVGCSKV PDINDVGLME DRATLRISSQ HIANWLRHGV VTQEQVLESL KRMAPVVDRQ NASDPLYRPL APDFDSNIAF QAALELVIEG TKQPNGYTEP VLHRRRREFK AKNGL //