ID   TTDA_ECOL5              Reviewed;         303 AA.
AC   Q0TD45;
DT   28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=L(+)-tartrate dehydratase subunit alpha;
DE            Short=L-TTD alpha;
DE            EC=4.2.1.32;
GN   Name=ttdA; OrderedLocusNames=ECP_3151;
OS   Escherichia coli O6:K15:H31 (strain 536 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=362663;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=536 / UPEC;
RX   PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x;
RA   Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U.,
RA   Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.;
RT   "Role of pathogenicity island-associated integrases in the genome
RT   plasticity of uropathogenic Escherichia coli strain 536.";
RL   Mol. Microbiol. 61:584-595(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}.
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DR   EMBL; CP000247; ABG71134.1; -; Genomic_DNA.
DR   RefSeq; WP_000986797.1; NC_008253.1.
DR   AlphaFoldDB; Q0TD45; -.
DR   SMR; Q0TD45; -.
DR   STRING; 362663.ECP_3151; -.
DR   EnsemblBacteria; ABG71134; ABG71134; ECP_3151.
DR   GeneID; 66673040; -.
DR   KEGG; ecp:ECP_3151; -.
DR   HOGENOM; CLU_041245_1_0_6; -.
DR   OMA; IETYPTH; -.
DR   Proteomes; UP000009182; 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_0000262697"
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;  32734 MW;  CBE29FEB6C47DB81 CRC64;
     MMSESNKQQA VNKLTEIVAN FTAMISTRMP DDVVDKLKQL KDAETSSMGK IIYHTMFDNM
     QKAIDLNRPA CQDTGEIMFF VKVGSRFPLL GELQSILKQA VEEATVKAPL RHNAVEIFDE
     VNTGKNTGSG VPWVTWDIIP DNDDAEIEVY MAGGGCTLPG RSKVLMPSEG YEGVVKFVFE
     NISTLAVNAC PPVLVGVGIA TSVETAAVLS RKAILRPIGS RHPNPKAAEL ELRLEEGLNR
     LGIGPQGLTG NSSVMGVHIE SAARHPSTIG VAVSTGCWAH RRGTLLVHAD LTFENLSHTR
     SAL