RIDA_PYRFU
ID RIDA_PYRFU Reviewed; 126 AA.
AC Q8U308;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase;
DE EC=3.5.99.10 {ECO:0000269|PubMed:22094463};
DE AltName: Full=Enamine/imine deaminase {ECO:0000303|PubMed:22094463};
GN Name=ridA {ECO:0000303|PubMed:22094463}; OrderedLocusNames=PF0668;
OS Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=186497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=10430560; DOI=10.1093/genetics/152.4.1299;
RA Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M.,
RA DiRuggiero J., Robb F.T.;
RT "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P.
RT horikoshii inferred from complete genomic sequences.";
RL Genetics 152:1299-1305(1999).
RN [2]
RP FUNCTION AS A DEAMINASE, AND CATALYTIC ACTIVITY.
RC STRAIN=ATCC 43587 / DSM 3638 / JCM 8422 / Vc1;
RX PubMed=22094463; DOI=10.1074/jbc.m111.304477;
RA Lambrecht J.A., Flynn J.M., Downs D.M.;
RT "The conserved YjgF protein family deaminates enamine/imine intermediates
RT of pyridoxal-5'-phosphate (PLP)-dependent enzyme reactions.";
RL J. Biol. Chem. 287:3454-3461(2012).
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. {ECO:0000269|PubMed:22094463}.
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:0000269|PubMed:22094463};
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.
CC -!- SUBUNIT: Homotrimer. {ECO:0000250|UniProtKB:P0AF93}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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DR EMBL; AE009950; AAL80792.1; -; Genomic_DNA.
DR RefSeq; WP_011011789.1; NZ_CP023154.1.
DR AlphaFoldDB; Q8U308; -.
DR SMR; Q8U308; -.
DR STRING; 186497.PF0668; -.
DR EnsemblBacteria; AAL80792; AAL80792; PF0668.
DR GeneID; 41712470; -.
DR KEGG; pfu:PF0668; -.
DR PATRIC; fig|186497.12.peg.703; -.
DR eggNOG; arCOG01630; Archaea.
DR HOGENOM; CLU_100715_7_3_2; -.
DR OMA; GSYFKEP; -.
DR OrthoDB; 90282at2157; -.
DR PhylomeDB; Q8U308; -.
DR BRENDA; 3.5.99.10; 5243.
DR Proteomes; UP000001013; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0120242; F:2-iminobutanoate deaminase activity; IDA: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 1: Evidence at protein level;
KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; Cytoplasm;
KW Detoxification; Hydrolase; Isoleucine biosynthesis; Reference proteome.
FT CHAIN 1..126
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /id="PRO_0000416002"
FT BINDING 103
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 118
FT /note="Important for catalytic activity at high pH"
FT /evidence="ECO:0000250|UniProtKB:Q7CP78"
SQ SEQUENCE 126 AA; 13907 MW; 9E2EF8B8D3094ACD CRC64;
MKEVIFAENA PKPIGPYSQA IKAGNFLFIA GQIPIDPKTG EIVKGDIKAQ TRQVLENIKA
ILEAAGYSLT DVVKVTVYLK DMNDFAKMNE VYAEYFGESK PARAAVEVSR LPKDVLIEIE
AIAYKE
