TDCF_ECOL6
ID TDCF_ECOL6 Reviewed; 129 AA.
AC P0AGL3; P42631;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Putative reactive intermediate deaminase TdcF;
DE EC=3.5.4.-;
GN Name=tdcF; OrderedLocusNames=c3871;
OS Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
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., Rasko D.,
RA Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA Donnenberg M.S., Blattner F.R.;
RT "Extensive mosaic structure revealed by the complete genome sequence of
RT uropathogenic Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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. {ECO:0000250}.
CC -!- PATHWAY: Amino-acid degradation; L-threonine degradation via propanoate
CC pathway.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAN82312.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE014075; AAN82312.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000719990.1; NC_004431.1.
DR AlphaFoldDB; P0AGL3; -.
DR SMR; P0AGL3; -.
DR STRING; 199310.c3871; -.
DR EnsemblBacteria; AAN82312; AAN82312; c3871.
DR GeneID; 66672986; -.
DR KEGG; ecc:c3871; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_1_6; -.
DR OMA; ATDKAPQ; -.
DR UniPathway; UPA00052; -.
DR Proteomes; UP000001410; Chromosome.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0070689; P:L-threonine catabolic process to propionate; IEA:UniProtKB-UniPathway.
DR GO; GO:0006566; P:threonine metabolic process; ISS: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 3: Inferred from homology;
KW Hydrolase; Pyridoxal phosphate.
FT CHAIN 1..129
FT /note="Putative reactive intermediate deaminase TdcF"
FT /id="PRO_0000170317"
FT BINDING 105..107
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 58
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 129 AA; 14007 MW; D5159CB729CDDB7B CRC64;
MKKIIETQRA PGAIGPYVQG VDLGSMVFTS GQIPVCPQTG EIPADVQDQA RLSLENVKAI
VVAAGLSVGD IIKMTVFITD LNDFATINEV YKQFFDEHQA TYPTRSCVQV ARLPKDVKLE
IEAIAVRSA