ID MASZ_GEOKA Reviewed; 727 AA. AC Q5KZR8; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-2005, sequence version 1. DT 27-MAR-2024, entry version 103. 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}; OrderedLocusNames=GK1533; OS Geobacillus kaustophilus (strain HTA426). OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus; OC Geobacillus thermoleovorans group. OX NCBI_TaxID=235909; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=HTA426; RX PubMed=15576355; DOI=10.1093/nar/gkh970; RA Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H., RA Matsui S., Uchiyama I.; RT "Thermoadaptation trait revealed by the genome sequence of thermophilic RT Geobacillus kaustophilus."; RL Nucleic Acids Res. 32:6292-6303(2004). 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; BA000043; BAD75818.1; -; Genomic_DNA. DR RefSeq; WP_011231029.1; NC_006510.1. DR AlphaFoldDB; Q5KZR8; -. DR SMR; Q5KZR8; -. DR STRING; 235909.GK1533; -. DR KEGG; gka:GK1533; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_9; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000001172; 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 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 Reference proteome; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..727 FT /note="Malate synthase G" FT /id="PRO_1000056902" 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 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 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 727 AA; 81148 MW; FB5BEA853C8B4CDB CRC64; MGEYVQKGNI QVAKVLYDFV NEELLPNSGL DQDKFWSDFG ALISDLTPRN KELLARRDEI QEKLNEWHKA HRGRFDFNEY KAFLTDIGYL EPEVEDFEIT TDNVDDEIAV QAGPQLVVPL TNARYALNAA NARWGSLYDA LYGTDAISEE DGAERGSSYN PVRGAKVIAY GRQFLDEAVP LAQYSHKDAV QYAIVDGQLV VTTEGGATTG LKEPEKFVGF QGDPQHPTAV LLKNNGLHIE IQIDREHAVG KTDQAGVKDI VLEAAVTTIM DGEDSVAAVD AEDKVLVYRN LFGLVKGDLT ATFEKNGKIM TRSLNPDRVY KTPDGGELVL PGRSLMFVRN VGHLMTNNAI LHANGEEVHE GIMDAVITSL IMKHSLIGNT RYLNSRKGSI YIVKPKMHGS AEVAFANELF DRVEDMLGLE RNTIKIGVMD EERRTSLNLK NCIYQVRDRI IFINTGFLDR TGDEIHTSME AGPMLRKNEM KSSTWLQAYE KSNVAVGLAA GFRGRAQIGK GMWAMPDLMA EMLKQKGAQL KAGANTAWVP SPTAATLHAL HYHQVNVSAV QSELANDRND YRDDMLQIPV VDHPQWTAEE IQEELDNNCQ SILGYVVRWI DQGIGCSKVP DIHNVGLMED RATLRISSQI LANWLHHGIC TKEQVLETLK RMAKVVDEQN AGDPNYRPMA PNYDDSVAFQ AACDLIFRGY EQPNGYTEPI LHRRRQEAKA KFAAIQQ //