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Database: UniProt
Entry: H3RJ58_PANSE
LinkDB: H3RJ58_PANSE
Original site: H3RJ58_PANSE 
ID   H3RJ58_PANSE            Unreviewed;       532 AA.
AC   H3RJ58;
DT   18-APR-2012, integrated into UniProtKB/TrEMBL.
DT   18-APR-2012, sequence version 1.
DT   24-JAN-2024, entry version 51.
DE   RecName: Full=Malate synthase {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
DE            EC=2.3.3.9 {ECO:0000256|ARBA:ARBA00012636, ECO:0000256|RuleBase:RU000555};
GN   Name=aceB {ECO:0000313|EMBL:EHT98315.1};
GN   ORFNames=CKS_4657 {ECO:0000313|EMBL:EHT98315.1}, DSJ_02945
GN   {ECO:0000313|EMBL:ARF48423.1};
OS   Pantoea stewartii subsp. stewartii DC283.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Pantoea.
OX   NCBI_TaxID=660596 {ECO:0000313|EMBL:EHT98315.1, ECO:0000313|Proteomes:UP000005050};
RN   [1] {ECO:0000313|EMBL:EHT98315.1, ECO:0000313|Proteomes:UP000005050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT98315.1,
RC   ECO:0000313|Proteomes:UP000005050};
RX   PubMed=22111898; DOI=10.1111/j.1365-2958.2011.07926.x;
RA   Wang X., Yang F., von Bodman S.B.;
RT   "The genetic and structural basis of two distinct terminal side branch
RT   residues in stewartan and amylovoran exopolysaccharides and their potential
RT   role in host adaptation.";
RL   Mol. Microbiol. 83:195-207(2012).
RN   [2] {ECO:0000313|EMBL:EHT98315.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=DC283 {ECO:0000313|EMBL:EHT98315.1};
RA   Biehl B.S., Ding Y., Dugan-Rocha S.P., Gibbs R.A., Glasner J.D., Kovar C.,
RA   Muzny D.M., Neeno-Eckwall E.C., Perna N.T., Qin X., von Bodman S.B.,
RA   Weinstock G.M.;
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:ARF48423.1, ECO:0000313|Proteomes:UP000192380}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DC283 {ECO:0000313|EMBL:ARF48423.1,
RC   ECO:0000313|Proteomes:UP000192380};
RA   Duong D.A., Stevens A.M., Jensen R.V.;
RT   "Complete Genome Assembly of Pantoea stewartii subsp. stewartii DC283, a
RT   Corn Pathogen.";
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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,
CC         ECO:0000256|RuleBase:RU000555};
CC   -!- PATHWAY: Carbohydrate metabolism; glyoxylate cycle; (S)-malate from
CC       isocitrate: step 2/2. {ECO:0000256|RuleBase:RU000555}.
CC   -!- SIMILARITY: Belongs to the malate synthase family.
CC       {ECO:0000256|ARBA:ARBA00006394, ECO:0000256|RuleBase:RU000555}.
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DR   EMBL; CP017581; ARF48423.1; -; Genomic_DNA.
DR   EMBL; AHIE01000037; EHT98315.1; -; Genomic_DNA.
DR   RefSeq; WP_006121533.1; NZ_CP017581.1.
DR   AlphaFoldDB; H3RJ58; -.
DR   STRING; 660596.DSJ_02945; -.
DR   KEGG; pstw:DSJ_02945; -.
DR   PATRIC; fig|660596.6.peg.4331; -.
DR   eggNOG; COG2225; Bacteria.
DR   OrthoDB; 9768429at2; -.
DR   UniPathway; UPA00703; UER00720.
DR   Proteomes; UP000005050; Unassembled WGS sequence.
DR   Proteomes; UP000192380; Chromosome.
DR   GO; GO:0004474; F:malate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006097; P:glyoxylate cycle; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   CDD; cd00727; malate_synt_A; 1.
DR   Gene3D; 3.20.20.360; Malate synthase, domain 3; 1.
DR   Gene3D; 1.20.1220.12; Malate synthase, domain III; 1.
DR   InterPro; IPR044856; Malate_synth_C_sf.
DR   InterPro; IPR011076; Malate_synth_sf.
DR   InterPro; IPR006252; Malate_synthA.
DR   InterPro; IPR019830; Malate_synthase_CS.
DR   InterPro; IPR001465; Malate_synthase_TIM.
DR   InterPro; IPR048355; MS_C.
DR   InterPro; IPR048356; MS_N.
DR   InterPro; IPR046363; MS_N_TIM-barrel_dom.
DR   NCBIfam; TIGR01344; malate_syn_A; 1.
DR   PANTHER; PTHR42902; MALATE SYNTHASE; 1.
DR   PANTHER; PTHR42902:SF1; MALATE SYNTHASE 1-RELATED; 1.
DR   Pfam; PF20659; MS_C; 1.
DR   Pfam; PF20656; MS_N; 1.
DR   Pfam; PF01274; MS_TIM-barrel; 1.
DR   PIRSF; PIRSF001363; Malate_synth; 1.
DR   SUPFAM; SSF51645; Malate synthase G; 1.
DR   PROSITE; PS00510; MALATE_SYNTHASE; 1.
PE   3: Inferred from homology;
KW   Acyltransferase {ECO:0000313|EMBL:EHT98315.1};
KW   Glyoxylate bypass {ECO:0000256|ARBA:ARBA00022435,
KW   ECO:0000256|RuleBase:RU000555};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU000555};
KW   Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW   ECO:0000256|RuleBase:RU000555}.
FT   DOMAIN          12..70
FT                   /note="Malate synthase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20656"
FT   DOMAIN          161..406
FT                   /note="Malate synthase TIM barrel"
FT                   /evidence="ECO:0000259|Pfam:PF01274"
FT   DOMAIN          412..530
FT                   /note="Malate synthase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF20659"
FT   ACT_SITE        165
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
FT   ACT_SITE        446
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001363-1"
SQ   SEQUENCE   532 AA;  60613 MW;  CA1614B61646E221 CRC64;
     MTDSVITHEL HFQKPFYHLE KQLLTEETVA FLQDLVIRFA PQRDTLLAAR QARQEKYDAG
     SLPDFEMETA SIREREWTIR GIPSDLRDRR VEITGPPDRK MVINALNANV KVFMADFEDS
     LAPTWEKLME GQQTLREAVA GTLSHTSETG KIYQLRADPA VLMCRVRGLH LSEKHVSWQG
     NAIPGGLFDF ALYFFHNVTN LLAKGSGPYF YLPKTESWQE AAWWREIFSF AEDRFDLARG
     TIKATVLIET LPAVFQMDEI LWNLRDHIVG LNCGRWDYIF SYIKTLREHE DRVLPDRQSV
     TMAQPFLDAY SRLLVKTCHR RGAFAMGGMS ALIPSKDSAR NQWVLQRVRE DKQREASNGH
     DGTWIAHPGL ADTAMAVFNQ ALGDHPNQLH VLRHEDAPVQ AEQLLAPCEG DRTEAGMRAN
     IRVALQYLEA WISGNGCVPI DGLMEDAATA EIARTSIWQW IHHKKTLRDG QQVTASLFQQ
     LLNDELHTLQ MNLGDKTFSS GRYEEAARLM AQITTENELV PFLTLPGYRL LP
//
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