RIDA_ECOLI
ID RIDA_ECOLI Reviewed; 128 AA.
AC P0AF93; P39330; P76806; Q2M664;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 126.
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=ridA; Synonyms=yjgF; OrderedLocusNames=b4243, JW5755;
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=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
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 [3]
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 [4]
RP PROTEIN SEQUENCE OF 2-13.
RC STRAIN=K12 / EMG2;
RX PubMed=9298646; DOI=10.1002/elps.1150180807;
RA Link A.J., Robison K., Church G.M.;
RT "Comparing the predicted and observed properties of proteins encoded in the
RT genome of Escherichia coli K-12.";
RL Electrophoresis 18:1259-1313(1997).
RN [5]
RP PROTEIN SEQUENCE OF 2-12.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RA Frutiger S., Hughes G.J., Pasquali C., Hochstrasser D.F.;
RL Submitted (FEB-1996) to UniProtKB.
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=B / BL21;
RX PubMed=10493123;
RX DOI=10.1002/(sici)1522-2683(19990801)20:11<2181::aid-elps2181>3.0.co;2-q;
RA Fountoulakis M., Takacs M.-F., Berndt P., Langen H., Takacs B.;
RT "Enrichment of low abundance proteins of Escherichia coli by hydroxyapatite
RT chromatography.";
RL Electrophoresis 20:2181-2195(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS), SUBUNIT, AND PUTATIVE SUBSTRATE
RP BINDING SITE.
RX PubMed=10595546; DOI=10.1110/ps.8.11.2428;
RA Volz K.;
RT "A test case for structure-based functional assignment: the 1.2-A crystal
RT structure of the yjgF gene product from Escherichia coli.";
RL Protein Sci. 8:2428-2437(1999).
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:0000269|PubMed:10595546}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA97140.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97140.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC77200.2; -; Genomic_DNA.
DR EMBL; AP009048; BAE78242.1; -; Genomic_DNA.
DR RefSeq; NP_418664.2; NC_000913.3.
DR RefSeq; WP_000047539.1; NZ_STEB01000013.1.
DR PDB; 1QU9; X-ray; 1.20 A; A/B/C=1-128.
DR PDBsum; 1QU9; -.
DR AlphaFoldDB; P0AF93; -.
DR SMR; P0AF93; -.
DR BioGRID; 4262720; 14.
DR DIP; DIP-36232N; -.
DR STRING; 511145.b4243; -.
DR DrugBank; DB03544; S-Phosphocysteine.
DR SWISS-2DPAGE; P0AF93; -.
DR jPOST; P0AF93; -.
DR PaxDb; P0AF93; -.
DR PRIDE; P0AF93; -.
DR EnsemblBacteria; AAC77200; AAC77200; b4243.
DR EnsemblBacteria; BAE78242; BAE78242; BAE78242.
DR GeneID; 66671838; -.
DR GeneID; 948771; -.
DR KEGG; ecj:JW5755; -.
DR KEGG; eco:b4243; -.
DR PATRIC; fig|511145.12.peg.4376; -.
DR EchoBASE; EB2415; -.
DR eggNOG; COG0251; Bacteria.
DR HOGENOM; CLU_100715_7_1_6; -.
DR InParanoid; P0AF93; -.
DR OMA; GSYFKEP; -.
DR PhylomeDB; P0AF93; -.
DR BioCyc; EcoCyc:G7877-MON; -.
DR BRENDA; 3.5.99.10; 2026.
DR EvolutionaryTrace; P0AF93; -.
DR PRO; PR:P0AF93; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0032991; C:protein-containing complex; IDA:EcoCyc.
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:0019239; F:deaminase activity; IDA:EcoCyc.
DR GO; GO:0051082; F:unfolded protein binding; IDA:EcoCyc.
DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW.
DR GO; GO:1901565; P:organonitrogen compound catabolic process; IBA:GO_Central.
DR GO; GO:0009636; P:response to toxic substance; IDA:EcoCyc.
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; Amino-acid biosynthesis;
KW Branched-chain amino acid biosynthesis; Cytoplasm; Detoxification;
KW Direct protein sequencing; Hydrolase; Isoleucine biosynthesis;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:9298646, ECO:0000269|Ref.5"
FT CHAIN 2..128
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /id="PRO_0000170321"
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"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:1QU9"
FT STRAND 18..22
FT /evidence="ECO:0007829|PDB:1QU9"
FT STRAND 24..29
FT /evidence="ECO:0007829|PDB:1QU9"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1QU9"
FT HELIX 46..63
FT /evidence="ECO:0007829|PDB:1QU9"
FT HELIX 68..70
FT /evidence="ECO:0007829|PDB:1QU9"
FT STRAND 71..79
FT /evidence="ECO:0007829|PDB:1QU9"
FT HELIX 81..83
FT /evidence="ECO:0007829|PDB:1QU9"
FT HELIX 84..97
FT /evidence="ECO:0007829|PDB:1QU9"
FT STRAND 104..109
FT /evidence="ECO:0007829|PDB:1QU9"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:1QU9"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1QU9"
SQ SEQUENCE 128 AA; 13612 MW; 4696BE30BAA71A15 CRC64;
MSKTIATENA PAAIGPYVQG VDLGNMIITS GQIPVNPKTG EVPADVAAQA RQSLDNVKAI
VEAAGLKVGD IVKTTVFVKD LNDFATVNAT YEAFFTEHNA TFPARSCVEV ARLPKDVKIE
IEAIAVRR
