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MASZ_BRUAB
ID   MASZ_BRUAB              Reviewed;         728 AA.
AC   Q57BM8;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=BruAb1_1636;
OS   Brucella abortus biovar 1 (strain 9-941).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=262698;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9-941;
RX   PubMed=15805518; DOI=10.1128/jb.187.8.2715-2726.2005;
RA   Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z.,
RA   Li L.-L., Kapur V., Alt D.P., Olsen S.C.;
RT   "Completion of the genome sequence of Brucella abortus and comparison to
RT   the highly similar genomes of Brucella melitensis and Brucella suis.";
RL   J. Bacteriol. 187:2715-2726(2005).
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; AE017223; AAX74956.1; -; Genomic_DNA.
DR   RefSeq; WP_002966937.1; NC_006932.1.
DR   AlphaFoldDB; Q57BM8; -.
DR   SMR; Q57BM8; -.
DR   EnsemblBacteria; AAX74956; AAX74956; BruAb1_1636.
DR   GeneID; 3788190; -.
DR   KEGG; bmb:BruAb1_1636; -.
DR   HOGENOM; CLU_028446_1_0_5; -.
DR   OMA; MAPGFDG; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000000540; Chromosome I.
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   Cytoplasm; Glyoxylate bypass; Magnesium; Metal-binding; Oxidation;
KW   Transferase; Tricarboxylic acid cycle.
FT   CHAIN           1..728
FT                   /note="Malate synthase G"
FT                   /id="PRO_1000056898"
FT   ACT_SITE        345
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   ACT_SITE        636
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         123
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         130..131
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         281
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         318
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         345
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         437
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         437
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         462..465
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         465
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         546
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   MOD_RES         622
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ   SEQUENCE   728 AA;  80044 MW;  A6301C27C4FF27FA CRC64;
     MGSAEKRNYV EIEGLAVAPE LVEFLAKEAA PGTGVEPEKF WKGFAAIIRD LTPKNRALLA
     KRDELQARID AWYKENRDKG YSQADYQQFL KDIGYLLPEG GAFSVSTTNV DPEITHIAGP
     QLVVPVMNAR YALNAANARW GSLYDALYGT DAISEADGAE KGKGYNPKRG EKVIAWAKNF
     LDESAPLSTG KWADVAGLAV NDGKLEIRLT DGSATTLKDE SQFKGYNGDA ASPTNVLLAK
     HNMHVDIVIN ADHPIGKTDP AHIADVVLES AISTIQDCED SIAVVDAEDK VAVYRNWLGL
     MNGKLEDTFE KNGKQMTRRL NGDRTYTAPD GSTLTLKGRS LMLVRNVGHL MTNPAILDAE
     GNEVPEGIMD AAFTSLIALH DIGPNGRHMN SREGSVYIVK PKMHGPEEVA FANEIFTRTE
     EMLGMKPNTL KIGIMDEERR TTVNLKEAIR AAKDRVVFIN TGFLDRTGDE IHTSMEAGPM
     IRKGDMKQAA WIGAYEQWNV DIGLECGLSG HAQIGKGMWA MPDMMAAMLE QKIAHPKAGA
     NTAWVPSPTA ATLHATHYHK IDVAAVQEKL KSRPRAKLDD ILSVPVAVRP NWTPDDIQHE
     IDNNAQGILG YVVRWIDQGV GCSKVPDINN VGLMEDRATL RISAQHIANW LYHGVVSEAQ
     VMETMKRMAA IVDKQNEGDP LYRPMAADFD KSIAFQAACD LVFKGREQPN GYTEPVLHRR
     RLELKQAS
 
 
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