ID TDCB_ECOL6 Reviewed; 329 AA.
AC P0AGF7; P05792;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 01-MAY-2013, entry version 54.
DE RecName: Full=L-threonine dehydratase catabolic TdcB;
DE EC=4.3.1.19;
DE AltName: Full=L-serine dehydratase;
DE EC=4.3.1.17;
DE AltName: Full=Threonine deaminase;
GN Name=tdcB; OrderedLocusNames=c3875;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
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.,
RA Rasko D., Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D.,
RA Mayhew G.F., Rose D.J., Zhou S., Schwartz D.C., Perna N.T.,
RA Mobley H.L.T., Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence
RT of uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate
CC and ammonia from threonine in a two-step reaction. The first step
CC involved a dehydration of threonine and a production of enamine
CC intermediates (aminocrotonate), which tautomerizes to its imine
CC form (iminobutyrate). Both intermediates are unstable and short-
CC lived. The second step is the nonenzymatic hydrolysis of the
CC enamine/imine intermediates to form 2-ketobutyrate and free
CC ammonia. In the low water environment of the cell, the second step
CC is accelerated by RidA. TdcB also dehydrates serine to yield
CC pyruvate via analogous enamine/imine intermediates (By
CC similarity).
CC -!- CATALYTIC ACTIVITY: L-threonine = 2-oxobutanoate + NH(3).
CC -!- CATALYTIC ACTIVITY: L-serine = pyruvate + NH(3).
CC -!- COFACTOR: Pyridoxal phosphate (By similarity).
CC -!- ENZYME REGULATION: Each protein molecule can bind up to four
CC molecules of AMP, which act as an allosteric activator to the
CC enzyme (By similarity).
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via
CC propanoate pathway; propanoate from L-threonine: step 1/4.
CC -!- SUBUNIT: In the native structure, TdcB is in a dimeric form,
CC whereas in the TdcB-AMP complex, it exists in a tetrameric form
CC (dimer of dimers) (By similarity).
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
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DR EMBL; AE014075; AAN82316.1; -; Genomic_DNA.
DR RefSeq; NP_755742.1; NC_004431.1.
DR ProteinModelPortal; P0AGF7; -.
DR SMR; P0AGF7; 2-325.
DR STRING; 199310.c3875; -.
DR EnsemblBacteria; AAN82316; AAN82316; c3875.
DR GeneID; 1040111; -.
DR KEGG; ecc:c3875; -.
DR PATRIC; 18285534; VBIEscCol75197_3649.
DR HOGENOM; HOG000046972; -.
DR KO; K01754; -.
DR OMA; DTPCVES; -.
DR ProtClustDB; PRK08638; -.
DR UniPathway; UPA00052; UER00507.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IEA:EC.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IEA:EC.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR001926; Trp_syn_b_sub_like_PLP_eny_SF.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; PyrdxlP-dep_enz_bsu; 1.
DR TIGRFAMs; TIGR01127; ilvA_1Cterm; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 3: Inferred from homology;
KW Allosteric enzyme; Complete proteome; Lyase; Nucleotide-binding;
KW Pyridoxal phosphate.
FT CHAIN 1 329 L-threonine dehydratase catabolic TdcB.
FT /FTId=PRO_0000185584.
FT NP_BIND 53 54 AMP (By similarity).
FT NP_BIND 119 120 AMP (By similarity).
FT BINDING 88 88 AMP (By similarity).
FT BINDING 314 314 AMP (By similarity).
FT MOD_RES 58 58 N6-(pyridoxal phosphate)lysine (By
FT similarity).
SQ SEQUENCE 329 AA; 35232 MW; E7DF018FCCF743B1 CRC64;
MHITYDLPVA IDDIIEAKQR LAGRIYKTGM PRSNYFSERC KGEIFLKFEN MQRTGSFKIR
GAFNKLSSLT DAEKRKGVVA CSAGNHAQGV SLSCAMLGID GKVVMPKGAP KSKVAATCDY
SAEVVLHGDN FNDTIAKVSE IVEMEGRIFI PPYDDPKVIA GQGTIGLEIM EDLYDVDNVI
VPIGGGGLIA GIAVAIKSIN PTIRVIGVQS ENVHGMAASF HSGEITTHRT TGTLADGCDV
SRPGNLTYEI VRELVDDIVL VSEDEIRNSM IALIQRNKVV TEGAGALACA ALLSGKLDQY
IQNRKTVSII SGGNIDLSRV SQITGFVDA
//
