ID   FUMD_SHIFL              Reviewed;          69 AA.
AC   P0ACX8; P77274;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   22-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Fumarase D {ECO:0000250|UniProtKB:P0ACX5};
DE            EC=4.2.1.2 {ECO:0000250|UniProtKB:P0ACX5};
GN   Name=fumD {ECO:0000250|UniProtKB:P0ACX5}; Synonyms=ydhZ;
GN   OrderedLocusNames=SF1703, S1835;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
CC   -!- FUNCTION: In vitro catalyzes the addition of water to fumarate, forming
CC       malate. Cannot catalyze the reverse reaction. Cannot use the cis-isomer
CC       maleate as substrate. {ECO:0000250|UniProtKB:P0ACX5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(S)-malate = fumarate + H2O; Xref=Rhea:RHEA:12460,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15589, ChEBI:CHEBI:29806; EC=4.2.1.2;
CC         Evidence={ECO:0000250|UniProtKB:P0ACX5};
CC   -!- SIMILARITY: Belongs to the FumD family. {ECO:0000305}.
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DR   EMBL; AE005674; AAN43280.1; -; Genomic_DNA.
DR   EMBL; AE014073; AAP17167.1; -; Genomic_DNA.
DR   RefSeq; NP_707573.1; NC_004337.2.
DR   RefSeq; WP_000528342.1; NZ_WPGW01000025.1.
DR   AlphaFoldDB; P0ACX8; -.
DR   SMR; P0ACX8; -.
DR   STRING; 198214.SF1703; -.
DR   EnsemblBacteria; AAN43280; AAN43280; SF1703.
DR   EnsemblBacteria; AAP17167; AAP17167; S1835.
DR   GeneID; 1024874; -.
DR   GeneID; 66674432; -.
DR   KEGG; sfl:SF1703; -.
DR   KEGG; sfx:S1835; -.
DR   PATRIC; fig|198214.7.peg.2015; -.
DR   HOGENOM; CLU_2755438_0_0_6; -.
DR   OMA; ALYQEMC; -.
DR   OrthoDB; 1971938at2; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; Chromosome.
DR   GO; GO:0004333; F:fumarate hydratase activity; IEA:UniProtKB-EC.
DR   InterPro; IPR024493; FumD.
DR   Pfam; PF10965; DUF2767; 1.
PE   3: Inferred from homology;
KW   Lyase; Reference proteome.
FT   CHAIN           1..69
FT                   /note="Fumarase D"
FT                   /id="PRO_0000168985"
SQ   SEQUENCE   69 AA;  7907 MW;  A98BDA2AADEF5C32 CRC64;
     MGNRTKEDEL YREMCRVVGK VVLEMRDLGQ EPKHIVIAGV LRTALANKRI QRSELEKQAM
     ETVINALVK