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Database: UniProt
Entry: G5B054_HETGA
LinkDB: G5B054_HETGA
Original site: G5B054_HETGA 
ID   G5B054_HETGA            Unreviewed;       147 AA.
AC   G5B054;
DT   14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT   14-DEC-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=Bis(5'-nucleosyl)-tetraphosphatase [asymmetrical] {ECO:0000256|ARBA:ARBA00018911};
DE            EC=3.6.1.17 {ECO:0000256|ARBA:ARBA00012447};
DE   AltName: Full=Diadenosine 5',5'''-P1,P4-tetraphosphate asymmetrical hydrolase {ECO:0000256|ARBA:ARBA00032644};
DE   AltName: Full=Nucleoside diphosphate-linked moiety X motif 2 {ECO:0000256|ARBA:ARBA00029676};
GN   ORFNames=GW7_19846 {ECO:0000313|EMBL:EHB02665.1};
OS   Heterocephalus glaber (Naked mole rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Hystricomorpha; Bathyergidae;
OC   Heterocephalus.
OX   NCBI_TaxID=10181 {ECO:0000313|EMBL:EHB02665.1, ECO:0000313|Proteomes:UP000006813};
RN   [1] {ECO:0000313|EMBL:EHB02665.1, ECO:0000313|Proteomes:UP000006813}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=21993625; DOI=10.1038/nature10533;
RA   Kim E.B., Fang X., Fushan A.A., Huang Z., Lobanov A.V., Han L.,
RA   Marino S.M., Sun X., Turanov A.A., Yang P., Yim S.H., Zhao X.,
RA   Kasaikina M.V., Stoletzki N., Peng C., Polak P., Xiong Z., Kiezun A.,
RA   Zhu Y., Chen Y., Kryukov G.V., Zhang Q., Peshkin L., Yang L., Bronson R.T.,
RA   Buffenstein R., Wang B., Han C., Li Q., Chen L., Zhao W., Sunyaev S.R.,
RA   Park T.J., Zhang G., Wang J., Gladyshev V.N.;
RT   "Genome sequencing reveals insights into physiology and longevity of the
RT   naked mole rat.";
RL   Nature 479:223-227(2011).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + P(1),P(4)-bis(5'-guanosyl) tetraphosphate = GMP + GTP +
CC         2 H(+); Xref=Rhea:RHEA:22484, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57553, ChEBI:CHEBI:58115; EC=3.6.1.17;
CC         Evidence={ECO:0000256|ARBA:ARBA00001560};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end CoA-ribonucleoside in mRNA + H2O = (R)-4'-
CC         phosphopantetheine + a 5'-end phospho-adenosine-phospho-
CC         ribonucleoside in mRNA + 2 H(+); Xref=Rhea:RHEA:67592, Rhea:RHEA-
CC         COMP:15719, Rhea:RHEA-COMP:17276, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:61723, ChEBI:CHEBI:144051,
CC         ChEBI:CHEBI:172371; Evidence={ECO:0000256|ARBA:ARBA00029364};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67593;
CC         Evidence={ECO:0000256|ARBA:ARBA00029364};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 5'-end FAD-phospho-ribonucleoside in mRNA + H2O = a 5'-end
CC         phospho-adenosine-phospho-ribonucleoside in mRNA + FMN + 2 H(+);
CC         Xref=Rhea:RHEA:67588, Rhea:RHEA-COMP:15719, Rhea:RHEA-COMP:17275,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:144051, ChEBI:CHEBI:172372;
CC         Evidence={ECO:0000256|ARBA:ARBA00024504};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67589;
CC         Evidence={ECO:0000256|ARBA:ARBA00024504};
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|ARBA:ARBA00001968};
CC   -!- SIMILARITY: Belongs to the Nudix hydrolase family.
CC       {ECO:0000256|ARBA:ARBA00005582}.
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DR   EMBL; JH167728; EHB02665.1; -; Genomic_DNA.
DR   RefSeq; XP_004838472.1; XM_004838415.2.
DR   AlphaFoldDB; G5B054; -.
DR   STRING; 10181.G5B054; -.
DR   Ensembl; ENSHGLT00100022436; ENSHGLP00100022204; ENSHGLG00100016344.
DR   GeneID; 101699878; -.
DR   KEGG; hgl:101699878; -.
DR   CTD; 318; -.
DR   eggNOG; KOG2839; Eukaryota.
DR   InParanoid; G5B054; -.
DR   OMA; WRDYEQA; -.
DR   OrthoDB; 196203at2759; -.
DR   Proteomes; UP000006813; Unassembled WGS sequence.
DR   Bgee; ENSHGLG00000007868; Expressed in heart and 10 other cell types or tissues.
DR   GO; GO:0004081; F:bis(5'-nucleosyl)-tetraphosphatase (asymmetrical) activity; IEA:UniProtKB-EC.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   CDD; cd03428; Ap4A_hydrolase_human_like; 1.
DR   Gene3D; 3.90.79.10; Nucleoside Triphosphate Pyrophosphohydrolase; 1.
DR   InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR   InterPro; IPR020084; NUDIX_hydrolase_CS.
DR   InterPro; IPR000086; NUDIX_hydrolase_dom.
DR   InterPro; IPR003565; Tetra_PHTase.
DR   PANTHER; PTHR21340:SF0; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE [ASYMMETRICAL]; 1.
DR   PANTHER; PTHR21340; DIADENOSINE 5,5-P1,P4-TETRAPHOSPHATE PYROPHOSPHOHYDROLASE MUTT; 1.
DR   Pfam; PF00293; NUDIX; 1.
DR   PRINTS; PR01405; TETRPHPHTASE.
DR   SUPFAM; SSF55811; Nudix; 1.
DR   PROSITE; PS51462; NUDIX; 1.
DR   PROSITE; PS00893; NUDIX_BOX; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006813}.
FT   DOMAIN          1..139
FT                   /note="Nudix hydrolase"
FT                   /evidence="ECO:0000259|PROSITE:PS51462"
SQ   SEQUENCE   147 AA;  16802 MW;  F5885ACA06B044C6 CRC64;
     MALRACGLII FRRHLIPKMD NSTIQFLLLQ ASDGIHHWTP PKGHVDPGEN DLETALRETW
     EEAGIEAGQL TIIEGFRKEL NYVARGKPKT VIYWLAEVKD CNVEIRLSHE HQAYRWLGLE
     EACQLAQFKE MKAAFQEGHQ FLCSTAS
//
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