NUD11_BOVIN
ID NUD11_BOVIN Reviewed; 164 AA.
AC Q58CW0;
DT 05-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 2.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=Diphosphoinositol polyphosphate phosphohydrolase 3-beta {ECO:0000250|UniProtKB:Q96G61};
DE Short=DIPP-3-beta;
DE Short=DIPP3-beta;
DE EC=3.6.1.52 {ECO:0000250|UniProtKB:Q96G61};
DE AltName: Full=Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase 3-beta;
DE AltName: Full=Diadenosine hexaphosphate hydrolase (AMP-forming);
DE EC=3.6.1.60 {ECO:0000250|UniProtKB:Q96G61};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 11;
DE Short=Nudix motif 11;
GN Name=NUDT11 {ECO:0000250|UniProtKB:Q96G61}; Synonyms=DIPP3B;
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].
RX PubMed=16305752; DOI=10.1186/1471-2164-6-166;
RA Harhay G.P., Sonstegard T.S., Keele J.W., Heaton M.P., Clawson M.L.,
RA Snelling W.M., Wiedmann R.T., Van Tassell C.P., Smith T.P.L.;
RT "Characterization of 954 bovine full-CDS cDNA sequences.";
RL BMC Genomics 6:166-166(2005).
CC -!- FUNCTION: Cleaves a beta-phosphate from the diphosphate groups in PP-
CC InsP5 (diphosphoinositol pentakisphosphate), suggesting that it may
CC play a role in signal transduction. Also able to catalyze the
CC hydrolysis of dinucleoside oligophosphates, with Ap6A and Ap5A being
CC the preferred substrates. The major reaction products are ADP and p4a
CC from Ap6A and ADP and ATP from Ap5A. Also able to hydrolyze 5-
CC phosphoribose 1-diphosphate. {ECO:0000250|UniProtKB:Q96G61}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=diphospho-myo-inositol polyphosphate + H2O = myo-inositol
CC polyphosphate + phosphate.; EC=3.6.1.52;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(6)-bis(5'-adenosyl) hexaphosphate = adenosine 5'-
CC pentaphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32047,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:63740,
CC ChEBI:CHEBI:63813, ChEBI:CHEBI:456215; EC=3.6.1.60;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + P(1),P(5)-bis(5'-adenosyl) pentaphosphate = adenosine
CC 5'-tetraphosphate + AMP + 2 H(+); Xref=Rhea:RHEA:32051,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:58450,
CC ChEBI:CHEBI:62041, ChEBI:CHEBI:456215; EC=3.6.1.60;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000250|UniProtKB:Q96G61};
CC Note=Binds 3 Mg(2+) or Mn(2+) ions per subunit. Mn(2+) may be the true
CC cofactor in vivo. {ECO:0000250|UniProtKB:Q96G61};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. DIPP subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAX46684.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; BT021837; AAX46684.1; ALT_FRAME; mRNA.
DR RefSeq; NP_001030565.2; NM_001035488.2.
DR AlphaFoldDB; Q58CW0; -.
DR SMR; Q58CW0; -.
DR STRING; 9913.ENSBTAP00000049572; -.
DR PaxDb; Q58CW0; -.
DR GeneID; 616931; -.
DR KEGG; bta:616931; -.
DR CTD; 170685; -.
DR eggNOG; KOG2839; Eukaryota.
DR InParanoid; Q58CW0; -.
DR OrthoDB; 1324716at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0034431; F:bis(5'-adenosyl)-hexaphosphatase activity; IBA:GO_Central.
DR GO; GO:0034432; F:bis(5'-adenosyl)-pentaphosphatase activity; IBA:GO_Central.
DR GO; GO:0008486; F:diphosphoinositol-polyphosphate diphosphatase activity; IBA:GO_Central.
DR GO; GO:0000298; F:endopolyphosphatase activity; IBA:GO_Central.
DR GO; GO:0052842; F:inositol diphosphate pentakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0052840; F:inositol diphosphate tetrakisphosphate diphosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0050072; F:m7G(5')pppN diphosphatase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:1901911; P:adenosine 5'-(hexahydrogen pentaphosphate) catabolic process; IBA:GO_Central.
DR GO; GO:1901909; P:diadenosine hexaphosphate catabolic process; IBA:GO_Central.
DR GO; GO:1901907; P:diadenosine pentaphosphate catabolic process; IBA:GO_Central.
DR GO; GO:0071543; P:diphosphoinositol polyphosphate metabolic process; IBA:GO_Central.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Hydrolase; Magnesium; Manganese; Metal-binding;
KW Reference proteome.
FT CHAIN 1..164
FT /note="Diphosphoinositol polyphosphate phosphohydrolase 3-
FT beta"
FT /id="PRO_0000057064"
FT DOMAIN 17..144
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT REGION 144..164
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 50..71
FT /note="Nudix box"
FT ACT_SITE 68
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 9
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 17..19
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 38..40
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 49
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 65
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 69
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 89..91
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 115
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
FT BINDING 133
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:O95989"
SQ SEQUENCE 164 AA; 18519 MW; 335256116E97AE72 CRC64;
MKCKPNQTRT YDPEGFKKRA ACLCFRSERE DEVLLVSSSR YPDRWIVPGG GMEPEEEPGG
AAVREVFEEA GVKGKLGRLL GNFEQNQDRK HRTYVYVLTV TEILEDWEDS VSIGRKREWF
KVEDAIKVLQ CHKPVHAEYL QKLKLGGSPT NGNSVAPSPP EGDP
