ID F6INB4_9SPHN Unreviewed; 704 AA. AC F6INB4; DT 27-JUL-2011, integrated into UniProtKB/TrEMBL. DT 27-JUL-2011, sequence version 1. DT 24-JAN-2024, entry version 70. 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=PP1Y_AT20390 {ECO:0000313|EMBL:CCA92916.1}; OS Novosphingobium sp. PP1Y. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales; OC Sphingomonadaceae; Novosphingobium. OX NCBI_TaxID=702113 {ECO:0000313|EMBL:CCA92916.1, ECO:0000313|Proteomes:UP000009242}; RN [1] {ECO:0000313|EMBL:CCA92916.1, ECO:0000313|Proteomes:UP000009242} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=sp. PP1Y {ECO:0000313|Proteomes:UP000009242}; RX PubMed=21685292; DOI=10.1128/JB.05349-11; RA D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L., Notomista E., RA Paolella G., Di Donato A., Salvatore F.; RT "De novo sequencing and assembly of the whole genome of Novosphingobium sp. RT strain PP1Y."; RL J. Bacteriol. 193:4296-4296(2011). 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, ECO:0000256|HAMAP- CC 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 --------------------------------------------------------------------------- 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; FR856862; CCA92916.1; -; Genomic_DNA. DR RefSeq; WP_013833231.1; NC_015580.1. DR AlphaFoldDB; F6INB4; -. DR KEGG; npp:PP1Y_AT20390; -. DR eggNOG; COG2225; Bacteria. DR HOGENOM; CLU_028446_1_0_5; -. DR OrthoDB; 9762054at2; -. DR UniPathway; UPA00703; UER00720. DR Proteomes; UP000009242; 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 Acyltransferase {ECO:0000313|EMBL:CCA92916.1}; 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 Reference proteome {ECO:0000313|Proteomes:UP000009242}; 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 DOMAIN 18..72 FT /note="Malate synthase N-terminal" FT /evidence="ECO:0000259|Pfam:PF20656" FT DOMAIN 158..193 FT /note="Malate synthase G alpha-beta insertion" FT /evidence="ECO:0000259|Pfam:PF20658" FT DOMAIN 315..544 FT /note="Malate synthase TIM barrel" FT /evidence="ECO:0000259|Pfam:PF01274" FT DOMAIN 569..650 FT /note="Malate synthase C-terminal" FT /evidence="ECO:0000259|Pfam:PF20659" FT ACT_SITE 318 FT /note="Proton acceptor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT ACT_SITE 609 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641, FT ECO:0000256|PIRSR:PIRSR601465-50" FT BINDING 118 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 125..126 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 254 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 291 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 318 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 410 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 410 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 435..438 FT /ligand="glyoxylate" FT /ligand_id="ChEBI:CHEBI:36655" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 438 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT BINDING 519 FT /ligand="acetyl-CoA" FT /ligand_id="ChEBI:CHEBI:57288" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" FT MOD_RES 595 FT /note="Cysteine sulfenic acid (-SOH)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00641" SQ SEQUENCE 704 AA; 76484 MW; CDA840251055D982 CRC64; MTQRVERSGL QIDAGLAAFV EEKVLAPIGQ DTDAFWSGFA QLLARFAPRN RELLEKRDHL QSQIDAWHMS RAGRPIEQGE YQAFLQDIGY LVPEPEVFSI GTRNVDPEIA TMAGPQLVVP VLNARFLLNA ANARWGSLYD AFYGTDALDA APAQGKGYDP VRGAAVIAEG RKFLDKALPL ASGSWADVDS LEVTLVDPDQ CVGETRKGCL FKSNGLHIEI VVDPSSQVGA TDKAGISDIV LEAALTTIVD LEDSVAAVDA EDKLLAYSNW LGVIRGDLTD TFEKGGQTLT RELAGNKVVT VPTGEAQELP GRSLLFVRNV GHLMTNPAIL LPDGSEIPEG IMDAVITSAI SAQDVKGMTR YGNSRKGSIY IVKPKMHGPE ECSFTNDLFD AVEDLLQLPR NTVKVGVMDE ERRTSANLAA CIHAVKDRIV FINTGFLDRT GDEIHTSMRA GPMIRKSAIK GSTWIAAYEK RNVAIGLRHG LSGVAQIGKG MWAAPDMMRD MMEQKVGHPR TGANTAWVPS PTAATLHAMH YHEVDVFGLR EGIAAEEIPG LDLLLQIPLA DGANWSEDEV REELENNAQG LLGYVVRWID QGVGCSKVPD INDVGLMEDR ATLRISSQHM ANWLLHGVCT EAQVMDALKR MAEKVDAQNA GDPLYAPMAG NWDTSLAFKA ACDLVFKGVE QPSGYTEPLL HAWRLKKKSA LVTA //