ID   MASZ_AGRFC              Reviewed;         731 AA.
AC   Q8UJ85;
DT   30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   30-APR-2003, sequence version 2.
DT   27-MAR-2024, entry version 116.
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};
GN   OrderedLocusNames=Atu0047; ORFNames=AGR_C_78;
OS   Agrobacterium fabrum (strain C58 / ATCC 33970) (Agrobacterium tumefaciens
OS   (strain C58)).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Agrobacterium;
OC   Agrobacterium tumefaciens complex.
OX   NCBI_TaxID=176299;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743193; DOI=10.1126/science.1066804;
RA   Wood D.W., Setubal J.C., Kaul R., Monks D.E., Kitajima J.P., Okura V.K.,
RA   Zhou Y., Chen L., Wood G.E., Almeida N.F. Jr., Woo L., Chen Y.,
RA   Paulsen I.T., Eisen J.A., Karp P.D., Bovee D. Sr., Chapman P.,
RA   Clendenning J., Deatherage G., Gillet W., Grant C., Kutyavin T., Levy R.,
RA   Li M.-J., McClelland E., Palmieri A., Raymond C., Rouse G.,
RA   Saenphimmachak C., Wu Z., Romero P., Gordon D., Zhang S., Yoo H., Tao Y.,
RA   Biddle P., Jung M., Krespan W., Perry M., Gordon-Kamm B., Liao L., Kim S.,
RA   Hendrick C., Zhao Z.-Y., Dolan M., Chumley F., Tingey S.V., Tomb J.-F.,
RA   Gordon M.P., Olson M.V., Nester E.W.;
RT   "The genome of the natural genetic engineer Agrobacterium tumefaciens
RT   C58.";
RL   Science 294:2317-2323(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C58 / ATCC 33970;
RX   PubMed=11743194; DOI=10.1126/science.1066803;
RA   Goodner B., Hinkle G., Gattung S., Miller N., Blanchard M., Qurollo B.,
RA   Goldman B.S., Cao Y., Askenazi M., Halling C., Mullin L., Houmiel K.,
RA   Gordon J., Vaudin M., Iartchouk O., Epp A., Liu F., Wollam C., Allinger M.,
RA   Doughty D., Scott C., Lappas C., Markelz B., Flanagan C., Crowell C.,
RA   Gurson J., Lomo C., Sear C., Strub G., Cielo C., Slater S.;
RT   "Genome sequence of the plant pathogen and biotechnology agent
RT   Agrobacterium tumefaciens C58.";
RL   Science 294:2323-2328(2001).
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   -!- SEQUENCE CAUTION:
CC       Sequence=AAK85871.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE007869; AAK85871.1; ALT_INIT; Genomic_DNA.
DR   PIR; AH2582; AH2582.
DR   PIR; F97364; F97364.
DR   RefSeq; NP_353086.1; NC_003062.2.
DR   AlphaFoldDB; Q8UJ85; -.
DR   SMR; Q8UJ85; -.
DR   STRING; 176299.Atu0047; -.
DR   EnsemblBacteria; AAK85871; AAK85871; Atu0047.
DR   KEGG; atu:Atu0047; -.
DR   PATRIC; fig|176299.10.peg.47; -.
DR   eggNOG; COG2225; Bacteria.
DR   HOGENOM; CLU_028446_1_0_5; -.
DR   OrthoDB; 9762054at2; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000000813; Chromosome circular.
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..731
FT                   /note="Malate synthase G"
FT                   /id="PRO_0000166879"
FT   ACT_SITE        346
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   ACT_SITE        637
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         125
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         132..133
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         282
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         319
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         346
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         438
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         438
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         463..466
FT                   /ligand="glyoxylate"
FT                   /ligand_id="ChEBI:CHEBI:36655"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         466
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   BINDING         547
FT                   /ligand="acetyl-CoA"
FT                   /ligand_id="ChEBI:CHEBI:57288"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
FT   MOD_RES         623
FT                   /note="Cysteine sulfenic acid (-SOH)"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00641"
SQ   SEQUENCE   731 AA;  79520 MW;  69F304D5D6F8EFFB CRC64;
     MPSEYKEAHV SRTDKFGLSI DDRLYAFLTD EVLPGTGLDS ETFFEGFSAI VHELSPKNRE
     LLAKRDALQE KIDGWYRENG APSDFDAYEA FLKEIGYLLP EGPGFKVETN NVDPEIAVVA
     GPQLVVPVMN ARYALNAANA RWGSLYDALY GTDAISDADG AEKGRGYNPK RGDKVIAWAR
     NFLDESAPLE TGSWSDVTGF NIADGLLQLA IGAATTGLKD AVQFKGFSGE AAKPATILLG
     KNGLHTEIVI DPSTEIGKSD RAGISDVILE SALTTIMDCE DSVAAVDAED KVLVYGNWLG
     LMRGDLTEAV SKGGNTFTRR LNPDRYYTAP DGSALTLPGR SLMLVRNVGH LMTNPAILDR
     DGRDVPEGIM DAVVTALIAL YDVGPSGRRQ NSRAGSMYVV KPKMHGPEEV AFANEIFARV
     ENLVGMAPNT MKMGIMDEER RTTVNLKESI RAAKDRVVFI NTGFLDRTGD EIHTSMEAGP
     MIRKGDMKQA AWIAAYENWN VDIGLECGLS GHAQIGKGMW AMPDLMAAML EQKIAHPKAG
     ANTAWVPSPT AATLHATHYH KVDVAAVQEG LKSRGRAKLS DILSVPVAPR PNWTPEEIQR
     ELDNNAQGIL GYVVRWVDQG VGCSKVPDIN NIGLMEDRAT LRISAQHMAN WLRHGVVTEA
     QIIKTMKRMA AVVDTQNAGD PAYLPMASDF DGSVAFQAAV ELVLKGREQP NGYTEPVLHR
     RRLELKAKQA G
//