ID   MASZ_NITWN              Reviewed;         741 AA.
AC   Q3SNX3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2005, sequence version 1.
DT   03-AUG-2022, entry version 108.
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=Nwi_2765;
OS   Nitrobacter winogradskyi (strain ATCC 25391 / DSM 10237 / CIP 104748 /
OS   NCIMB 11846 / Nb-255).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Nitrobacter.
OX   NCBI_TaxID=323098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25391 / DSM 10237 / CIP 104748 / NCIMB 11846 / Nb-255;
RX   PubMed=16517654; DOI=10.1128/aem.72.3.2050-2063.2006;
RA   Starkenburg S.R., Chain P.S.G., Sayavedra-Soto L.A., Hauser L., Land M.L.,
RA   Larimer F.W., Malfatti S.A., Klotz M.G., Bottomley P.J., Arp D.J.,
RA   Hickey W.J.;
RT   "Genome sequence of the chemolithoautotrophic nitrite-oxidizing bacterium
RT   Nitrobacter winogradskyi Nb-255.";
RL   Appl. Environ. Microbiol. 72:2050-2063(2006).
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;
CC         Evidence={ECO:0000255|HAMAP-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}.
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DR   EMBL; CP000115; ABA06018.1; -; Genomic_DNA.
DR   RefSeq; WP_011315963.1; NC_007406.1.
DR   AlphaFoldDB; Q3SNX3; -.
DR   SMR; Q3SNX3; -.
DR   STRING; 323098.Nwi_2765; -.
DR   PRIDE; Q3SNX3; -.
DR   EnsemblBacteria; ABA06018; ABA06018; Nwi_2765.
DR   KEGG; nwi:Nwi_2765; -.
DR   eggNOG; COG2225; Bacteria.
DR   HOGENOM; CLU_028446_1_0_5; -.
DR   OMA; MAPGFDG; -.
DR   OrthoDB; 322024at2; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000002531; 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; 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   Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation;
KW   Reference proteome; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..741
FT                   /note="Malate synthase G"
FT                   /id="PRO_1000056914"
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   741 AA;  81247 MW;  304959E432A852B2 CRC64;
     MNRIDAHGLK IAPVLFDFIA GEATLRTGIK PDAFWAGLAA IVRDLGPRNR ELLAVRDRLQ
     ARIDDWHRIH KDTPFDISAY TAFLTEIGYL EPEPETRQIE TANVDDEIGK ICGPQLVVPL
     TNARYALNAA NARWGSLYDA LYGTDAIARE AGEAKGYDKA RGDKVIARAK AFLDMATPLA
     NGAHADVAGY SVLNGRLSVT LRNGDTTGLK AETQFAGYQG DANAPSAILL VNHGLHIDIQ
     IDRAHPIGRH YSAGVADVII EAAISTILDM EDSVAAVDAD DKVLVYRNAL GLMNGTLTDT
     FEKSGKTLTR ALNPDRVYTA PDGGQLTLHG RSLLLIRNVG HHMFTDAVLD QRGAEIPEGL
     LDAAISGLLA IHDINGVSKR RNSRSGSLYL VKPKMHGPDE VALTCELFAR VEAMLGLREN
     TLKIGIMDEE RRTTVNLNAC IQTASKRVCF INTGFLDRTG DEIHTSMEAG PMIRKGEMKT
     QPWIKAYEDW NVDIGLIEGL PGRAQIGKGM WAAPDRMADM LAQKINHPEA GATTAWVPSP
     TAATLHALHY HQIDVRKRQQ ELKAGGRRAR LSDLLTIPVS HSNWPPEDVK QEIDNNCQGI
     LGYVVRWIDQ GVGCSKVPDI HDVGLMEDRA TLRISSQHLA NWLHHGVVTH DQVMDSFKRM
     AVIVDEQNAG DPLYKPMAPG FDSVAFKAAC DLVFRGREQP NGYTEHILTE RRREAKLMAQ
     AARAFSGEAD TGSPRENATR Q