RIDA_SHIFL
ID RIDA_SHIFL Reviewed; 128 AA.
AC P0AF95; P39330; P76806;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 97.
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=SF4247, S4509;
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: 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. May have a role in the purine metabolism (By similarity).
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=AAN45665.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP19453.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005674; AAN45665.2; ALT_INIT; Genomic_DNA.
DR EMBL; AE014073; AAP19453.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_709958.2; NC_004337.2.
DR RefSeq; WP_000047539.1; NZ_WPGW01000068.1.
DR AlphaFoldDB; P0AF95; -.
DR SMR; P0AF95; -.
DR STRING; 198214.SF4247; -.
DR EnsemblBacteria; AAN45665; AAN45665; SF4247.
DR EnsemblBacteria; AAP19453; AAP19453; S4509.
DR GeneID; 1026589; -.
DR GeneID; 66671838; -.
DR KEGG; sfl:SF4247; -.
DR KEGG; sfx:S4509; -.
DR PATRIC; fig|198214.7.peg.5007; -.
DR HOGENOM; CLU_100715_7_1_6; -.
DR OrthoDB; 1850770at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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; Reference proteome.
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_0000170323"
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
