ID A0A0S3F083_9SPHN Unreviewed; 161 AA.
AC A0A0S3F083;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=RNA pyrophosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00298};
DE EC=3.6.1.- {ECO:0000256|HAMAP-Rule:MF_00298};
DE AltName: Full=(Di)nucleoside polyphosphate hydrolase {ECO:0000256|HAMAP-Rule:MF_00298};
GN Name=rppH {ECO:0000256|HAMAP-Rule:MF_00298};
GN Synonyms=nudH {ECO:0000256|HAMAP-Rule:MF_00298};
GN ORFNames=ATN00_12900 {ECO:0000313|EMBL:ALR21060.1};
OS Sphingobium baderi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1332080 {ECO:0000313|EMBL:ALR21060.1, ECO:0000313|Proteomes:UP000056968};
RN [1] {ECO:0000313|EMBL:ALR21060.1, ECO:0000313|Proteomes:UP000056968}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DE-13 {ECO:0000313|EMBL:ALR21060.1,
RC ECO:0000313|Proteomes:UP000056968};
RA Cheng M., Meng Q., Yang Y., Chu C., Yan X., He J., Li S.;
RT "A Two-component Flavoprotein Monooxygenase System MeaXY Responsible for
RT para-Hydroxylation of 2-Methyl-6-ethylaniline and 2,6-Diethylaniline in
RT Sphingobium baderi DE-13.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Accelerates the degradation of transcripts by removing
CC pyrophosphate from the 5'-end of triphosphorylated RNA, leading to a
CC more labile monophosphorylated state that can stimulate subsequent
CC ribonuclease cleavage. {ECO:0000256|HAMAP-Rule:MF_00298}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00298};
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. RppH subfamily.
CC {ECO:0000256|HAMAP-Rule:MF_00298}.
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DR EMBL; CP013264; ALR21060.1; -; Genomic_DNA.
DR RefSeq; WP_062065254.1; NZ_CP013264.1.
DR AlphaFoldDB; A0A0S3F083; -.
DR STRING; 1332080.ATN00_12900; -.
DR KEGG; sbd:ATN00_12900; -.
DR OrthoDB; 9816040at2; -.
DR Proteomes; UP000056968; Chromosome.
DR GO; GO:0016462; F:pyrophosphatase activity; IEA:UniProt.
DR CDD; cd03671; Ap4A_hydrolase_plant_like; 1.
DR Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR HAMAP; MF_00298; Nudix_RppH; 1.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR InterPro; IPR022927; RppH.
DR PANTHER; PTHR43046; GDP-MANNOSE MANNOSYL HYDROLASE; 1.
DR PANTHER; PTHR43046:SF12; GDP-MANNOSE MANNOSYL HYDROLASE; 1.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; Nudix; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00298};
KW Reference proteome {ECO:0000313|Proteomes:UP000056968}.
FT DOMAIN 11..155
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000259|PROSITE:PS51462"
FT MOTIF 45..66
FT /note="Nudix box"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00298"
SQ SEQUENCE 161 AA; 18562 MW; DE9C8033F30850AE CRC64;
MASMPKDEEL GYRPCVGIML VNMEGQVFVG QRIDNRAEAW QMPQGGIDDG EDAKAAALRE
LGEETGIHRK HVEIIAKARD EHFYDLPPEL VGQIWGGKYR GQRQIWFLAR FLGEDGDIDI
ETPHPEFRAW KWTAPETLPD LIVPFKRKLY RDILQEFQSL I
//
