ID   TTDA_ECOUT              Reviewed;         303 AA.
AC   Q1R6S0;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 75.
DE   RecName: Full=L(+)-tartrate dehydratase subunit alpha;
DE            Short=L-TTD alpha;
DE            EC=4.2.1.32;
GN   Name=ttdA; OrderedLocusNames=UTI89_C3497;
OS   Escherichia coli (strain UTI89 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=364106;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UTI89 / UPEC;
RX   PubMed=16585510; DOI=10.1073/pnas.0600938103;
RA   Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A.,
RA   Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S.,
RA   Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J.,
RA   Gordon J.I.;
RT   "Identification of genes subject to positive selection in uropathogenic
RT   strains of Escherichia coli: a comparative genomics approach.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000243; ABE08944.1; -; Genomic_DNA.
DR   RefSeq; WP_000986807.1; NC_007946.1.
DR   AlphaFoldDB; Q1R6S0; -.
DR   SMR; Q1R6S0; -.
DR   PRIDE; Q1R6S0; -.
DR   EnsemblBacteria; ABE08944; ABE08944; UTI89_C3497.
DR   KEGG; eci:UTI89_C3497; -.
DR   HOGENOM; CLU_041245_1_0_6; -.
DR   OMA; IETYPTH; -.
DR   Proteomes; UP000001952; 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_0000262699"
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