TDCF_ECOLI
ID TDCF_ECOLI Reviewed; 129 AA.
AC P0AGL2; P42631; Q2M995;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Putative reactive intermediate deaminase TdcF;
DE EC=3.5.4.-;
GN Name=tdcF; Synonyms=yhaR; OrderedLocusNames=b3113, JW5521;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
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 [2]
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 [3]
RP GENE NAME.
RX PubMed=9484901; DOI=10.1046/j.1365-2958.1998.00696.x;
RA Hesslinger C., Fairhurst S.A., Sawers G.;
RT "Novel keto acid formate-lyase and propionate kinase enzymes are components
RT of an anaerobic pathway in Escherichia coli that degrades L-threonine to
RT propionate.";
RL Mol. Microbiol. 27:477-492(1998).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOGS,
RP AND SUBUNIT.
RX PubMed=17506874; DOI=10.1186/1472-6807-7-30;
RA Burman J.D., Stevenson C.E., Sawers R.G., Lawson D.M.;
RT "The crystal structure of Escherichia coli TdcF, a member of the highly
RT conserved YjgF/YER057c/UK114 family.";
RL BMC Struct. Biol. 7:30-30(2007).
CC -!- FUNCTION: May be a post-translational regulator that controls the
CC metabolic fate of L-threonine or the potentially toxic intermediate 2-
CC ketobutyrate.
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17506874}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA57917.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U18997; AAA57917.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC76148.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE77161.1; -; Genomic_DNA.
DR PIR; F65100; F65100.
DR RefSeq; NP_417583.4; NC_000913.3.
DR RefSeq; WP_000719990.1; NZ_SSZK01000007.1.
DR PDB; 2UYJ; X-ray; 2.35 A; A/B/C=1-129.
DR PDB; 2UYK; X-ray; 1.60 A; A/B/C=1-129.
DR PDB; 2UYN; X-ray; 1.60 A; A/B/C=1-129.
DR PDB; 2UYP; X-ray; 2.44 A; A/B/C=1-129.
DR PDBsum; 2UYJ; -.
DR PDBsum; 2UYK; -.
DR PDBsum; 2UYN; -.
DR PDBsum; 2UYP; -.
DR AlphaFoldDB; P0AGL2; -.
DR SMR; P0AGL2; -.
DR BioGRID; 4259264; 16.
DR DIP; DIP-48213N; -.
DR STRING; 511145.b3113; -.
DR ChEMBL; CHEMBL3309027; -.
DR jPOST; P0AGL2; -.
DR PaxDb; P0AGL2; -.
DR PRIDE; P0AGL2; -.
DR EnsemblBacteria; AAC76148; AAC76148; b3113.
DR EnsemblBacteria; BAE77161; BAE77161; BAE77161.
DR GeneID; 66672986; -.
DR GeneID; 947624; -.
DR KEGG; ecj:JW5521; -.
DR KEGG; eco:b3113; -.
DR PATRIC; fig|511145.12.peg.3207; -.
DR EchoBASE; EB2611; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_1_6; -.
DR InParanoid; P0AGL2; -.
DR OMA; ATDKAPQ; -.
DR PhylomeDB; P0AGL2; -.
DR BioCyc; EcoCyc:G7626-MON; -.
DR UniPathway; UPA00052; -.
DR EvolutionaryTrace; P0AGL2; -.
DR PRO; PR:P0AGL2; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0019239; F:deaminase activity; IBA:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IBA:GO_Central.
DR GO; GO:0006566; P:threonine metabolic process; IDA:UniProtKB.
DR Gene3D; 3.30.1330.40; -; 1.
DR InterPro; IPR006056; RidA.
DR InterPro; IPR019897; RidA_CS.
DR InterPro; IPR035959; RutC-like_sf.
DR InterPro; IPR006175; YjgF/YER057c/UK114.
DR PANTHER; PTHR11803; PTHR11803; 1.
DR Pfam; PF01042; Ribonuc_L-PSP; 1.
DR SUPFAM; SSF55298; SSF55298; 1.
DR TIGRFAMs; TIGR00004; TIGR00004; 1.
DR PROSITE; PS01094; UPF0076; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Pyridoxal phosphate; Reference proteome.
FT CHAIN 1..129
FT /note="Putative reactive intermediate deaminase TdcF"
FT /id="PRO_0000170316"
FT BINDING 105..107
FT /ligand="substrate"
FT BINDING 120
FT /ligand="substrate"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2UYK"
FT STRAND 8..10
FT /evidence="ECO:0007829|PDB:2UYP"
FT STRAND 14..16
FT /evidence="ECO:0007829|PDB:2UYN"
FT STRAND 19..22
FT /evidence="ECO:0007829|PDB:2UYK"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:2UYK"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:2UYK"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:2UYK"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:2UYK"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:2UYK"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:2UYK"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:2UYK"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:2UYK"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:2UYK"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:2UYK"
SQ SEQUENCE 129 AA; 14007 MW; D5159CB729CDDB7B CRC64;
MKKIIETQRA PGAIGPYVQG VDLGSMVFTS GQIPVCPQTG EIPADVQDQA RLSLENVKAI
VVAAGLSVGD IIKMTVFITD LNDFATINEV YKQFFDEHQA TYPTRSCVQV ARLPKDVKLE
IEAIAVRSA
