ID MASZ_RHOPT Reviewed; 724 AA. AC B3QKU1; DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot. DT 02-SEP-2008, sequence version 1. DT 27-MAR-2024, entry version 86. 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=Rpal_4697; OS Rhodopseudomonas palustris (strain TIE-1). OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Nitrobacteraceae; Rhodopseudomonas. OX NCBI_TaxID=395960; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=TIE-1; RG US DOE Joint Genome Institute; RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Emerson D., RA Newman D.K., Roden E., Richardson P.; RT "Complete sequence of Rhodopseudomonas palustris TIE-1."; RL Submitted (MAY-2008) 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; CP001096; ACF03188.1; -; Genomic_DNA. DR RefSeq; WP_012497463.1; NC_011004.1. DR AlphaFoldDB; B3QKU1; -. DR SMR; B3QKU1; -. DR KEGG; rpt:Rpal_4697; -. DR HOGENOM; CLU_028446_1_0_5; -. DR OrthoDB; 9762054at2; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001725; Chromosome. 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 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_1000130897" FT ACT_SITE 337 FT /note="Proton acceptor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT ACT_SITE 628 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 273 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 310 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" FT BINDING 337 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 614 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00641" SQ SEQUENCE 724 AA; 78535 MW; 0102198CFF95EEFC CRC64; MNRIDAHGLK IAPVLFDFIA KEAAPKTGIA PDVFWAGLAA IVRDLAPKTR ALLKTRDDLQ AKIDAWHLAN KGKKQDMAAY TAFLKEIGYL LPEPPTVPVE TANIDEEIGK LCGPQLVVPL SNARYALNAA NARWGSLYDA FYGTDAIPQE ATQAKGYDKA RGDKVIAKAK AFLDQAAPLA TGSHSDVTGY SVIAGQLSAK LKSGNATGLK KPAQFAGFRG DAANPSAVLL VNNGLHIEIK IDRANTIGKD DPAGVADLVI ESAVSTILDM EDSVAAVDAD DKVLIYRNTL GLMDGTLSES FEKGGKTVTR ALNGDRTYTA PDGKEISLHG RSLLLMRNVG HHMWTDAVLD SDGQEIPEGF LDAAVSGLIA IHDLKHLGKT RNSRTGSVYI VKPKMHGPDE VALTVELFGR VETMLGLTAN TLKVGIMDEE RRTTVNLKAC IQNASKRIVF INTGFLDRTG DEIHTSMEAG PMIRKNEMKA QPWIKAYEDW NVDTGLVDGL PGHAQIGKGM WAAPDKMADM LAQKIGHPQA GATTAWVPSP TAATLHALHY HQVDVIARQQ ELAKGGPRAK LEDILTIPVS NSNWAPDDVR QEIDNNCQGI LGYVVRWIDQ GVGCSKVPDI HDVGLMEDRA TLRISSQHLA NWLHHGVVTK DQVLDSLKRM AVIVDKQNEG DALYRPIAPD FDGVAFEAAC DLIFKGRAQP NGYTEYILHE RRREAKAAHL ESAR //