RIDA_BOVIN
ID RIDA_BOVIN Reviewed; 137 AA.
AC Q3T114;
DT 11-JUL-2006, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=2-iminobutanoate/2-iminopropanoate deaminase {ECO:0000250|UniProtKB:P52758};
DE EC=3.5.99.10 {ECO:0000250|UniProtKB:P52758};
DE AltName: Full=Translation inhibitor L-PSP ribonuclease {ECO:0000250|UniProtKB:P52759};
DE EC=3.1.-.- {ECO:0000250|UniProtKB:P52759};
GN Name=RIDA {ECO:0000250|UniProtKB:P52758};
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Crossbred X Angus; TISSUE=Ileum;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the hydrolytic deamination of enamine/imine
CC intermediates that form during the course of normal metabolism. May
CC facilitate the release of ammonia from these potentially toxic reactive
CC metabolites, reducing their impact on cellular components. It may act
CC on enamine/imine intermediates formed by several types of pyridoxal-5'-
CC phosphate-dependent dehydratases including L-threonine dehydratase.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- FUNCTION: Also promotes endoribonucleolytic cleavage of some
CC transcripts by promoting recruitment of the ribonuclease P/MRP complex.
CC Acts by bridging YTHDF2 and the ribonuclease P/MRP complex. RIDA/HRSP12
CC binds to N6-methyladenosine (m6A)-containing mRNAs containing a 5'-
CC GGUUC-3' motif: cooperative binding of RIDA/HRSP12 and YTHDF2 to such
CC transcripts lead to recruitment of the ribonuclease P/MRP complex and
CC subsequent endoribonucleolytic cleavage.
CC {ECO:0000250|UniProtKB:P52758}.
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:P52758};
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 Evidence={ECO:0000250|UniProtKB:P52758};
CC -!- SUBUNIT: Homotrimer. Interacts with YTHDF2.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P52758}. Nucleus
CC {ECO:0000250|UniProtKB:P52758}. Peroxisome
CC {ECO:0000250|UniProtKB:P52759}. Mitochondrion
CC {ECO:0000250|UniProtKB:P52759}. Note=Mostly cytoplasmic but, in less
CC differentiated cells occasionally nuclear.
CC {ECO:0000250|UniProtKB:P52758}.
CC -!- SIMILARITY: Belongs to the RutC family. {ECO:0000305}.
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DR EMBL; BC102164; AAI02165.1; -; mRNA.
DR RefSeq; NP_001029380.1; NM_001034208.2.
DR AlphaFoldDB; Q3T114; -.
DR SMR; Q3T114; -.
DR STRING; 9913.ENSBTAP00000016718; -.
DR PaxDb; Q3T114; -.
DR PeptideAtlas; Q3T114; -.
DR PRIDE; Q3T114; -.
DR Ensembl; ENSBTAT00000016718; ENSBTAP00000016718; ENSBTAG00000012595.
DR GeneID; 504390; -.
DR KEGG; bta:504390; -.
DR CTD; 10247; -.
DR VEuPathDB; HostDB:ENSBTAG00000012595; -.
DR VGNC; VGNC:33964; RIDA.
DR eggNOG; KOG2317; Eukaryota.
DR GeneTree; ENSGT00420000029792; -.
DR HOGENOM; CLU_100715_7_1_1; -.
DR InParanoid; Q3T114; -.
DR OMA; GSYFKEP; -.
DR OrthoDB; 1435276at2759; -.
DR TreeFam; TF105775; -.
DR Reactome; R-BTA-8849175; Threonine catabolism.
DR Proteomes; UP000009136; Chromosome 14.
DR Bgee; ENSBTAG00000012595; Expressed in monocyte and 103 other tissues.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005777; C:peroxisome; ISS:UniProtKB.
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; IBA:GO_Central.
DR GO; GO:0016892; F:endoribonuclease activity, producing 3'-phosphomonoesters; ISS:UniProtKB.
DR GO; GO:0003729; F:mRNA binding; ISS:UniProtKB.
DR GO; GO:0006629; P:lipid metabolic process; IEA:UniProtKB-KW.
DR GO; GO:0006402; P:mRNA catabolic process; ISS:UniProtKB.
DR GO; GO:0061157; P:mRNA destabilization; ISS:UniProtKB.
DR GO; GO:0017148; P:negative regulation of translation; ISS:UniProtKB.
DR GO; GO:1901565; P:organonitrogen compound catabolic 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 2: Evidence at transcript level;
KW Acetylation; Cytoplasm; Hydrolase; Lipid metabolism; Mitochondrion;
KW Nucleus; Peroxisome; Phosphoprotein; Reference proteome; RNA-binding.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P80601"
FT CHAIN 2..137
FT /note="2-iminobutanoate/2-iminopropanoate deaminase"
FT /id="PRO_0000245864"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000250|UniProtKB:P80601"
FT MOD_RES 13
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 67
FT /note="N6-succinyllysine"
FT /evidence="ECO:0000250|UniProtKB:P52760"
FT MOD_RES 74
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P52758"
FT MOD_RES 136
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:P52758"
SQ SEQUENCE 137 AA; 14272 MW; A519B7F146C51547 CRC64;
MSSLVRKIIS TAKAPAAIGP YSQAVLVDRT IYISGQLGMD PASGQLVPGG VAEEAKQALT
NIGEILKAAG CDFTNVVKAT VLLADINDFS TVNDVYKQYF QSSFPARAAY QVAALPKGGR
VEIEAIAVQG PLTTASL
