ID A0A7X4G9B2_9GAMM Unreviewed; 726 AA. AC A0A7X4G9B2; DT 02-JUN-2021, integrated into UniProtKB/TrEMBL. DT 02-JUN-2021, sequence version 1. DT 25-MAY-2022, entry version 4. DE RecName: Full=Malate synthase G {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; DE EC=2.3.3.9 {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; GN Name=glcB {ECO:0000256|HAMAP-Rule:MF_00641}; GN ORFNames=GLW02_05130 {ECO:0000313|EMBL:MYL74177.1}; OS Halomonas sp. 22501_18_FS. OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales; OC Halomonadaceae; Halomonas. OX NCBI_TaxID=2665505 {ECO:0000313|EMBL:MYL74177.1, ECO:0000313|Proteomes:UP000462486}; RN [1] {ECO:0000313|EMBL:MYL74177.1, ECO:0000313|Proteomes:UP000462486} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=22501_18_FS {ECO:0000313|EMBL:MYL74177.1, RC ECO:0000313|Proteomes:UP000462486}; RA Furrow R.E.; RT "Genome sequences of 17 halophilic strains isolated from different RT environments."; RL Submitted (NOV-2019) 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:0000256|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; CC Evidence={ECO:0000256|ARBA:ARBA00001699, ECO:0000256|HAMAP- CC Rule:MF_00641, ECO:0000256|RuleBase:RU003572}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000256|ARBA:ARBA00001946, CC ECO:0000256|HAMAP-Rule:MF_00641}; CC -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from CC isocitrate: step 2/2. {ECO:0000256|HAMAP-Rule:MF_00641, CC ECO:0000256|RuleBase:RU003572}. CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00641}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00641, CC ECO:0000256|RuleBase:RU003572}. CC -!- SIMILARITY: Belongs to the malate synthase family. GlcB subfamily. CC {ECO:0000256|HAMAP-Rule:MF_00641, ECO:0000256|RuleBase:RU003572}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00641}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:MYL74177.1}. 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; WMFD01000003; MYL74177.1; -; Genomic_DNA. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000462486; Unassembled WGS sequence. 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; 1.20.1220.12; -; 1. DR Gene3D; 3.20.20.360; -; 2. 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. DR InterPro; IPR006253; Malate_synthG. DR InterPro; IPR046363; MS_N_TIM-barrel_dom. DR PANTHER; PTHR42739; PTHR42739; 1. DR Pfam; PF01274; Malate_synthase; 1. DR SUPFAM; SSF51645; SSF51645; 1. DR TIGRFAMs; TIGR01345; malate_syn_G; 1. PE 3: Inferred from homology; KW Acyltransferase {ECO:0000313|EMBL:MYL74177.1}; KW Coiled coil {ECO:0000256|SAM:Coils}; KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00641}; KW Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|HAMAP-Rule:MF_00641}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Oxidation {ECO:0000256|ARBA:ARBA00023097, ECO:0000256|HAMAP-Rule:MF_00641}; KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP- KW Rule:MF_00641}; KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532, ECO:0000256|HAMAP- KW Rule:MF_00641}. FT REGION 125..126 FT /note="Acetyl-CoA binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT REGION 457..460 FT /note="Glyoxylate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT COILED 50..70 FT /evidence="ECO:0000256|SAM:Coils" FT ACT_SITE 340 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT ACT_SITE 632 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT METAL 432 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT METAL 460 FT /note="Magnesium" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 118 FT /note="Acetyl-CoA; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 276 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 313 FT /note="Acetyl-CoA" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 340 FT /note="Glyoxylate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 432 FT /note="Glyoxylate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 541 FT /note="Acetyl-CoA; via carbonyl oxygen" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT MOD_RES 618 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" SQ SEQUENCE 726 AA; 80043 MW; CAE905CE699A639E CRC64; MTERVNAGGL QVARILYDFV NNEALPGTGV DADQFWNEFG RIVADMAPRN RELLKVRDEL QEKLDDWHRE HQGQSIDLNE YKTFLKDIGY LKPEGEDFTA TTENVDKEIA QVAGPQLVVP ISNARFALNA ANARWGSLYD AVYGSDIISE EGGATKGPGY NPVRGEKVIA YARAMLDESA PLASGSHADA TGYRVDGGQL KVTLNSGSEA SLKDPAQFVG YKGSESEPEG ILLVRNGVHF EIQIDASHPI GKDDAAHVKD VLMESALTTI MDCEDSVAAV DAEDKTGVYR NWLGLMQGNL EESFEKGGKT VTRSMAGDRE YLDASGKPMS LHGRSLMLVR NVGHLMTNDA ILDVDGNEVP EGLMDGMITS LIAIHDLKGN NRVGNSRTGS VYIVKPKMHG PDEVAFTNEL FGRVEDALGM KRNTLKVGVM DEERRTTVNL KECIRQAKDR IIFINTGFLD RTGDEIHTSM EAGPVIRKGE MKQAPWMTSY EDWNVDIGLE TGLKGRAQIG KGMWPMPDKL AAMMDAKISH PKAGANTAWV PSPTAATLHA IHYHQVNVMD VQGELSKRER ASLDNILTVP LMKDPSVLSQ EDIKQELDNN AQGILGYVVR WIEEGVGCSK VPDINDVGLM EDRATLRIAS QLLCNWLYHG ICTEEQVMET LKRMAKVVDR QNEGDPNYIP MADDFEGNVA FQAACDLIFK GREQPSGYTE PLLHAYRRKA KAKYGQ //