ID   TDCF_SHIFL              Reviewed;         129 AA.
AC   P0AGL4; P42631;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Putative reactive intermediate deaminase TdcF;
DE            EC=3.5.4.-;
GN   Name=tdcF; OrderedLocusNames=SF3153, S3365;
OS   Shigella flexneri.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=623;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=301 / Serotype 2a;
RX   PubMed=12384590; DOI=10.1093/nar/gkf566;
RA   Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA   Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA   Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA   Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT   "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT   through comparison with genomes of Escherichia coli K12 and O157.";
RL   Nucleic Acids Res. 30:4432-4441(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX   PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA   Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA   Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA   Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT   "Complete genome sequence and comparative genomics of Shigella flexneri
RT   serotype 2a strain 2457T.";
RL   Infect. Immun. 71:2775-2786(2003).
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}.
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DR   EMBL; AE005674; AAN44624.2; -; Genomic_DNA.
DR   EMBL; AE014073; AAP18438.1; -; Genomic_DNA.
DR   RefSeq; NP_708917.2; NC_004337.2.
DR   RefSeq; WP_000719990.1; NZ_WPGW01000077.1.
DR   AlphaFoldDB; P0AGL4; -.
DR   SMR; P0AGL4; -.
DR   STRING; 198214.SF3153; -.
DR   PRIDE; P0AGL4; -.
DR   EnsemblBacteria; AAN44624; AAN44624; SF3153.
DR   EnsemblBacteria; AAP18438; AAP18438; S3365.
DR   GeneID; 1027187; -.
DR   GeneID; 66672986; -.
DR   KEGG; sfl:SF3153; -.
DR   KEGG; sfx:S3365; -.
DR   PATRIC; fig|198214.7.peg.3743; -.
DR   HOGENOM; CLU_100715_7_1_6; -.
DR   OMA; ATDKAPQ; -.
DR   OrthoDB; 1850770at2; -.
DR   UniPathway; UPA00052; -.
DR   Proteomes; UP000001006; Chromosome.
DR   Proteomes; UP000002673; 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; Reference proteome.
FT   CHAIN           1..129
FT                   /note="Putative reactive intermediate deaminase TdcF"
FT                   /id="PRO_0000170318"
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