ID MASZ_PSEA8 Reviewed; 725 AA. AC B7V467; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 1. DT 27-MAR-2024, entry version 82. 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=PLES_04781; OS Pseudomonas aeruginosa (strain LESB58). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=557722; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=LESB58; RX PubMed=19047519; DOI=10.1101/gr.086082.108; RA Winstanley C., Langille M.G.I., Fothergill J.L., Kukavica-Ibrulj I., RA Paradis-Bleau C., Sanschagrin F., Thomson N.R., Winsor G.L., Quail M.A., RA Lennard N., Bignell A., Clarke L., Seeger K., Saunders D., Harris D., RA Parkhill J., Hancock R.E.W., Brinkman F.S.L., Levesque R.C.; RT "Newly introduced genomic prophage islands are critical determinants of in RT vivo competitiveness in the Liverpool epidemic strain of Pseudomonas RT aeruginosa."; RL Genome Res. 19:12-23(2009). 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; FM209186; CAW25205.1; -; Genomic_DNA. DR RefSeq; WP_003105217.1; NC_011770.1. DR AlphaFoldDB; B7V467; -. DR SMR; B7V467; -. DR KEGG; pag:PLES_04781; -. DR HOGENOM; CLU_028446_1_0_6; -. 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..725 FT /note="Malate synthase G" FT /id="PRO_1000130894" 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; 78632 MW; CEC503219946E5CE CRC64; MTERVQVGGL QVAKVLFDFV NNEAIPGTGV SADTFWTGAE AVINDLAPKN KALLAKRDEL QAKIDGWHQA RAGQAHDAAA YKAFLEEIGY LLPEAEDFQA GTQNVDDEIA RMAGPQLVVP VMNARFALNA SNARWGSLYD ALYGTDVISE EGGAEKGKGY NKVRGDKVIA FARAFLDEAA PLESGSHVDA TSYSVKNGAL VVALKNGSET GLKNAGQFLA FQGDAAKPQA VLLKHNGLHF EIQIDPSSPV GQTDAAGVKD VLMEAALTTI MDCEDSVAAV DADDKVVIYR NWLGLMKGDL AEEVSKGGST FTRTMNPDRV YTRADGSELT LHGRSLLFVR NVGHLMTNDA ILDKDGNEVP EGIQDGLFTS LIAIHDLNGN TSRKNSRTGS VYIVKPKMHG PEEAAFTNEL FGRVEDVLGL PRNTLKVGIM DEERRTTVNL KACIKAAKDR VVFINTGFLD RTGDEIHTSM EAGAVVRKGA MKSEKWIGAY ENNNVDVGLA TGLQGKAQIG KGMWAMPDLM AAMLEQKIGH PLAGANTAWV PSPTAATLHA LHYHKVDVFA RQAELAKRTP ASVDDILTIP LAPNTNWTAE EIKNEVDNNA QGILGYVVRW IDQGVGCSKV PDINDVGLME DRATLRISSQ LLANWLRHGV ISQEQVVESL KRMAVVVDRQ NASDPSYRPM APNFDDNVAF QAALELVVEG TRQPNGYTEP VLHRRRREFK AKNGL //