ID   TTDA_ECOL6              Reviewed;         303 AA.
AC   Q8FDG8;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=L(+)-tartrate dehydratase subunit alpha;
DE            Short=L-TTD alpha;
DE            EC=4.2.1.32;
GN   Name=ttdA; OrderedLocusNames=c3812;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2R,3R)-tartrate = H2O + oxaloacetate; Xref=Rhea:RHEA:15413,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:16452, ChEBI:CHEBI:30924; EC=4.2.1.32;
CC   -!- COFACTOR:
CC       Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC         Evidence={ECO:0000250|UniProtKB:P05847};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta subunits. {ECO:0000250}.
CC   -!- INDUCTION: Induced by tartrate, via TtdR. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}.
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DR   EMBL; AE014075; AAN82257.1; -; Genomic_DNA.
DR   RefSeq; WP_000986807.1; NC_004431.1.
DR   AlphaFoldDB; Q8FDG8; -.
DR   SMR; Q8FDG8; -.
DR   STRING; 199310.c3812; -.
DR   EnsemblBacteria; AAN82257; AAN82257; c3812.
DR   KEGG; ecc:c3812; -.
DR   eggNOG; COG1951; Bacteria.
DR   HOGENOM; CLU_041245_1_0_6; -.
DR   OMA; IETYPTH; -.
DR   BioCyc; ECOL199310:C3812-MON; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0008730; F:L(+)-tartrate dehydratase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008152; P:metabolic process; IEA:UniProt.
DR   InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat.
DR   Pfam; PF05681; Fumerase; 1.
DR   TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Lyase; Metal-binding.
FT   CHAIN           1..303
FT                   /note="L(+)-tartrate dehydratase subunit alpha"
FT                   /id="PRO_0000262698"
FT   BINDING         71
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000250|UniProtKB:E9AE57"
FT   BINDING         190
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000250|UniProtKB:E9AE57"
FT   BINDING         277
FT                   /ligand="iron-sulfur cluster"
FT                   /ligand_id="ChEBI:CHEBI:30408"
FT                   /evidence="ECO:0000250|UniProtKB:E9AE57"
SQ   SEQUENCE   303 AA;  32706 MW;  720CA4CDBA8B6136 CRC64;
     MMSESNKQQA VNKLTEIVAN FTAMISTRMP DDVVDKLKQL KDAETSSMGK IIYHTMFDNM
     QKAIDLNRPA CQDTGEIMFF VKVGSRFPLL GELQSILKQA VEEATVKAPL RHNAVEIFDE
     VNTGKNTGSG VPWVTWDIVP DGDDAEIEVY MAGGGCTLPG RSKVLMPSEG YEGVVKFVFE
     NISTLAVNAC PPVLVGVGIA TSVETAAVLS RKAILRPIGS RHPNPKAAEL ELRLEEGLNR
     LGIGPQGLTG NSSVMGVHIE SAARHPSTIG VAVSTGCWAH RRGTLRVHAD LTFENLSHTR
     SAL