ID   RIDA_ECOL6              Reviewed;         128 AA.
AC   P0AF94; P39330; P76806;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase;
DE            EC=3.5.99.10 {ECO:0000250|UniProtKB:Q7CP78};
DE   AltName: Full=Enamine/imine deaminase;
GN   Name=yjgF; OrderedLocusNames=c5342;
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: Accelerates the release of ammonia from reactive
CC       enamine/imine intermediates of the PLP-dependent threonine dehydratase
CC       (IlvA) in the low water environment of the cell. It catalyzes the
CC       deamination of enamine/imine intermediates to yield 2-ketobutyrate and
CC       ammonia. It is required for the detoxification of reactive
CC       intermediates of IlvA due to their highly nucleophilic abilities.
CC       Involved in the isoleucine biosynthesis.
CC       {ECO:0000250|UniProtKB:Q7CP78}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-iminobutanoate + H2O = 2-oxobutanoate + NH4(+);
CC         Xref=Rhea:RHEA:39975, ChEBI:CHEBI:15377, ChEBI:CHEBI:16763,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:76545; EC=3.5.99.10;
CC         Evidence={ECO:0000250|UniProtKB:Q7CP78};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-iminopropanoate + H2O = NH4(+) + pyruvate;
CC         Xref=Rhea:RHEA:40671, ChEBI:CHEBI:15361, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:28938, ChEBI:CHEBI:44400; EC=3.5.99.10;
CC   -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2-
CC       oxobutanoate from L-threonine. {ECO:0000250|UniProtKB:Q7CP78}.
CC   -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0AF93}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN83763.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN83763.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000047539.1; NC_004431.1.
DR   AlphaFoldDB; P0AF94; -.
DR   SMR; P0AF94; -.
DR   STRING; 199310.c5342; -.
DR   PRIDE; P0AF94; -.
DR   EnsemblBacteria; AAN83763; AAN83763; c5342.
DR   GeneID; 66671838; -.
DR   KEGG; ecc:c5342; -.
DR   eggNOG; COG0251; Bacteria.
DR   HOGENOM; CLU_100715_7_1_6; -.
DR   OMA; GSYFKEP; -.
DR   Proteomes; UP000001410; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0120242; F:2-iminobutanoate deaminase activity; ISS:UniProtKB.
DR   GO; GO:0120243; F:2-iminopropanoate deaminase activity; IEA:RHEA.
DR   GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009636; P:response to toxic substance; IEA:UniProtKB-KW.
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   Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW   Detoxification; Hydrolase; Isoleucine biosynthesis.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000250"
FT   CHAIN           2..128
FT                   /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT                   /id="PRO_0000170322"
FT   ACT_SITE        107
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   BINDING         105
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7CP78"
FT   SITE            17
FT                   /note="Stabilizes the substrate"
FT                   /evidence="ECO:0000250|UniProtKB:Q7CP78"
FT   SITE            120
FT                   /note="Important for catalytic activity at high pH"
FT                   /evidence="ECO:0000250|UniProtKB:Q7CP78"
SQ   SEQUENCE   128 AA;  13612 MW;  4696BE30BAA71A15 CRC64;
     MSKTIATENA PAAIGPYVQG VDLGNMIITS GQIPVNPKTG EVPADVAAQA RQSLDNVKAI
     VEAAGLKVGD IVKTTVFVKD LNDFATVNAT YEAFFTEHNA TFPARSCVEV ARLPKDVKIE
     IEAIAVRR