TDCB_ECOLI
ID TDCB_ECOLI Reviewed; 329 AA.
AC P0AGF6; P05792; Q2M990;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=b3117, JW3088;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=3540965; DOI=10.1073/pnas.84.2.393;
RA Datta P., Goss T.J., Omnaas J.R., Patil R.V.;
RT "Covalent structure of biodegradative threonine dehydratase of Escherichia
RT coli: homology with other dehydratases.";
RL Proc. Natl. Acad. Sci. U.S.A. 84:393-397(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=2660107; DOI=10.1093/nar/17.10.3994;
RA Schweizer H., Datta P.;
RT "The complete nucleotide sequence of the tdc region of Escherichia coli.";
RL Nucleic Acids Res. 17:3994-3994(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 1-25.
RX PubMed=6751404; DOI=10.1016/0167-4838(82)90371-5;
RA Kim S.S., Datta P.;
RT "Chemical characterization of biodegradative threonine dehydratases from
RT two enteric bacteria.";
RL Biochim. Biophys. Acta 706:27-35(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 323-329.
RX PubMed=3053659; DOI=10.1128/jb.170.11.5352-5359.1988;
RA Goss T.J., Schweizer H.P., Datta P.;
RT "Molecular characterization of the tdc operon of Escherichia coli K-12.";
RL J. Bacteriol. 170:5352-5359(1988).
RN [7]
RP FUNCTION AS A THREONINE AND SERINE DEHYDRATASE, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND ACTIVITY REGULATION.
RX PubMed=15390404;
RA Wood W.A., Gunsalus I.C.;
RT "Serine and threonine desaminaes of Escherichia coli; activators for a
RT cell-free enzyme.";
RL J. Biol. Chem. 181:171-182(1949).
RN [8]
RP FUNCTION AS A THREONINE AND SERINE DEHYDRATASE, INDUCTION, AND ACTIVITY
RP REGULATION.
RX PubMed=13405870; DOI=10.1128/jb.73.1.105-112.1957;
RA Umbarger H.E., Brown B.;
RT "Threonine deamination in Escherichia coli. II. Evidence for two L-
RT threonine deaminases.";
RL J. Bacteriol. 73:105-112(1957).
RN [9]
RP REACTION MECHANISM, AND COFACTOR.
RX PubMed=5321308; DOI=10.1016/s0021-9258(18)97012-2;
RA Phillips A.T., Wood W.A.;
RT "The mechanism of action of 5'-adenylic acid-activated threonine
RT dehydrase.";
RL J. Biol. Chem. 240:4703-4709(1965).
RN [10]
RP FUNCTION IN CATABOLISM OF THREONINE.
RX PubMed=10388709; DOI=10.1128/aem.65.7.3100-3107.1999;
RA Guillouet S., Rodal A.A., An G., Lessard P.A., Sinskey A.J.;
RT "Expression of the Escherichia coli catabolic threonine dehydratase in
RT Corynebacterium glutamicum and its effect on isoleucine production.";
RL Appl. Environ. Microbiol. 65:3100-3107(1999).
RN [11]
RP REVIEW.
RX PubMed=17954980; DOI=10.1007/s12038-007-0121-1;
RA Simanshu D.K., Chittori S., Savithri H.S., Murthy M.R.;
RT "Structure and function of enzymes involved in the anaerobic degradation of
RT L-threonine to propionate.";
RL J. Biosci. 32:1195-1206(2007).
CC -!- FUNCTION: Catalyzes the anaerobic formation of alpha-ketobutyrate and
CC ammonia from threonine in a two-step reaction. The first step involved
CC a dehydration of threonine and a production of enamine intermediates
CC (aminocrotonate), which tautomerizes to its imine form (iminobutyrate).
CC Both intermediates are unstable and short-lived. The second step is the
CC nonenzymatic hydrolysis of the enamine/imine intermediates to form 2-
CC ketobutyrate and free ammonia. In the low water environment of the
CC cell, the second step is accelerated by RidA. TdcB also dehydrates
CC serine to yield pyruvate via analogous enamine/imine intermediates.
CC {ECO:0000269|PubMed:10388709, ECO:0000269|PubMed:13405870,
CC ECO:0000269|PubMed:15390404}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-threonine = 2-oxobutanoate + NH4(+); Xref=Rhea:RHEA:22108,
CC ChEBI:CHEBI:16763, ChEBI:CHEBI:28938, ChEBI:CHEBI:57926; EC=4.3.1.19;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-serine = NH4(+) + pyruvate; Xref=Rhea:RHEA:19169,
CC ChEBI:CHEBI:15361, ChEBI:CHEBI:28938, ChEBI:CHEBI:33384; EC=4.3.1.17;
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:5321308};
CC -!- ACTIVITY REGULATION: Each protein molecule can bind up to four
CC molecules of AMP, which act as an allosteric activator to the enzyme.
CC The enzyme is also inhibited by alpha-keto acids and other catabolites.
CC {ECO:0000269|PubMed:13405870, ECO:0000269|PubMed:15390404}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.30 uM for L-threonine (at 37 dregrees Celsius and at pH 7.8)
CC {ECO:0000269|PubMed:15390404};
CC KM=0.35 uM for L-serine (at 37 dregrees Celsius and at pH 7.8)
CC {ECO:0000269|PubMed:15390404};
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway; propanoate from L-threonine: step 1/4.
CC -!- SUBUNIT: In the native structure, TdcB is in a dimeric form, whereas in
CC the TdcB-AMP complex, it exists in a tetrameric form (dimer of dimers).
CC {ECO:0000250}.
CC -!- INDUCTION: In the absence of glucose and oxygen.
CC {ECO:0000269|PubMed:13405870}.
CC -!- SIMILARITY: Belongs to the serine/threonine dehydratase family.
CC {ECO:0000305}.
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DR EMBL; M21312; AAA24660.1; -; Genomic_DNA.
DR EMBL; X14430; CAA32593.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57921.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76152.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77166.1; -; Genomic_DNA.
DR EMBL; M23638; AAA24661.1; -; Genomic_DNA.
DR PIR; A26367; DWECTD.
DR RefSeq; NP_417587.1; NC_000913.3.
DR RefSeq; WP_000548347.1; NZ_STEB01000001.1.
DR AlphaFoldDB; P0AGF6; -.
DR SMR; P0AGF6; -.
DR BioGRID; 4262419; 22.
DR DIP; DIP-48063N; -.
DR IntAct; P0AGF6; 3.
DR STRING; 511145.b3117; -.
DR jPOST; P0AGF6; -.
DR PaxDb; P0AGF6; -.
DR PRIDE; P0AGF6; -.
DR EnsemblBacteria; AAC76152; AAC76152; b3117.
DR EnsemblBacteria; BAE77166; BAE77166; BAE77166.
DR GeneID; 66672982; -.
DR GeneID; 947633; -.
DR KEGG; ecj:JW3088; -.
DR KEGG; eco:b3117; -.
DR PATRIC; fig|1411691.4.peg.3613; -.
DR EchoBASE; EB0983; -.
DR eggNOG; COG1171; Bacteria.
DR HOGENOM; CLU_021152_4_2_6; -.
DR InParanoid; P0AGF6; -.
DR OMA; LIHPFDH; -.
DR PhylomeDB; P0AGF6; -.
DR BioCyc; EcoCyc:THREDEHYDCAT-MON; -.
DR BioCyc; MetaCyc:THREDEHYDCAT-MON; -.
DR SABIO-RK; P0AGF6; -.
DR UniPathway; UPA00052; UER00507.
DR PRO; PR:P0AGF6; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
DR GO; GO:0016597; F:amino acid binding; IDA:EcoliWiki.
DR GO; GO:0003941; F:L-serine ammonia-lyase activity; IDA:EcoCyc.
DR GO; GO:0004794; F:L-threonine ammonia-lyase activity; IDA:EcoCyc.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:EcoliWiki.
DR GO; GO:0004793; F:threonine aldolase activity; IDA:EcoliWiki.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IBA:GO_Central.
DR GO; GO:0006565; P:L-serine catabolic process; IDA:EcoCyc.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR GO; GO:0006567; P:threonine catabolic process; IDA:EcoCyc.
DR Gene3D; 3.40.50.1100; -; 2.
DR InterPro; IPR001926; PLP-dep.
DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS.
DR InterPro; IPR005789; Thr_deHydtase_catblc.
DR InterPro; IPR036052; Trypto_synt_PLP_dependent.
DR Pfam; PF00291; PALP; 1.
DR SUPFAM; SSF53686; SSF53686; 1.
DR TIGRFAMs; TIGR01127; ilvA_1Cterm; 1.
DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1.
PE 1: Evidence at protein level;
KW Allosteric enzyme; Direct protein sequencing; Lyase; Nucleotide-binding;
KW Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..329
FT /note="L-threonine dehydratase catabolic TdcB"
FT /id="PRO_0000185582"
FT BINDING 53..54
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 88
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 119..120
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT BINDING 314
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
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
