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DPNP_ORYSJ
ID   DPNP_ORYSJ              Reviewed;         358 AA.
AC   Q2QWT4; Q40639;
DT   24-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase;
DE            EC=3.1.3.7;
DE   AltName: Full=3'(2'),5-bisphosphonucleoside 3'(2')-phosphohydrolase;
DE   AltName: Full=DPNPase;
GN   OrderedLocusNames=Os12g0183300, LOC_Os12g08280;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16188032; DOI=10.1186/1741-7007-3-20;
RG   The rice chromosomes 11 and 12 sequencing consortia;
RT   "The sequence of rice chromosomes 11 and 12, rich in disease resistance
RT   genes and recent gene duplications.";
RL   BMC Biol. 3:20-20(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 159-358.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
CC   -!- FUNCTION: Converts adenosine 3'-phosphate 5'-phosphosulfate (PAPS) to
CC       adenosine 5'-phosphosulfate (APS) and 3'(2')-phosphoadenosine
CC       5'- phosphate (PAP) to AMP. Regulates the flux of sulfur in the sulfur-
CC       activation pathway by converting PAPS to APS (By similarity).
CC       {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=adenosine 3',5'-bisphosphate + H2O = AMP + phosphate;
CC         Xref=Rhea:RHEA:10040, ChEBI:CHEBI:15377, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:58343, ChEBI:CHEBI:456215; EC=3.1.3.7;
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by Ca(2+), Li(+), and Na(+) and
CC       activated by K(+). {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000305}.
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DR   EMBL; DP000011; ABA95973.1; -; Genomic_DNA.
DR   EMBL; AP008218; BAF29345.1; -; Genomic_DNA.
DR   EMBL; AP014968; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AK058937; -; NOT_ANNOTATED_CDS; mRNA.
DR   AlphaFoldDB; Q2QWT4; -.
DR   SMR; Q2QWT4; -.
DR   STRING; 4530.OS12T0183300-01; -.
DR   PaxDb; Q2QWT4; -.
DR   PRIDE; Q2QWT4; -.
DR   eggNOG; KOG1528; Eukaryota.
DR   HOGENOM; CLU_033446_3_1_1; -.
DR   InParanoid; Q2QWT4; -.
DR   Proteomes; UP000000763; Chromosome 12.
DR   Proteomes; UP000059680; Chromosome 12.
DR   Genevisible; Q2QWT4; OS.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0042578; F:phosphoric ester hydrolase activity; IBA:GO_Central.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IEA:InterPro.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
DR   InterPro; IPR006239; Bisphos_HAL2.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   TIGRFAMs; TIGR01330; bisphos_HAL2; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Magnesium; Metal-binding; Reference proteome.
FT   CHAIN           1..358
FT                   /note="3'(2'),5'-bisphosphate nucleotidase"
FT                   /id="PRO_0000142535"
FT   BINDING         78
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         78
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         140
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         142..145
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         142
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   358 AA;  37480 MW;  EFE813C18BEDB5FD CRC64;
     MSQAAGNPYA AELAAAKKAV TLAARLCQAV QKDILQSGVQ SKADQSPVTV ADYGSQILVS
     LVLKMEAPAS SSFSMVAEED SEELRKEGAE EILENITELV NETIVDDGTY SIYFSKEGIL
     SAIDDGKSEG GPSGRHWVLD PIDGTKGFLR GDQYAIALAL LDEGKVVLGV LACPNLSLGS
     IGNLNGGSSG DQVGALFSAT IGCGAEVESL QGSPAQKISV CSIDNPVEAS FFESYEGAHS
     LRDLTGSIAE KLGVQAPPVR IDSQAKYGAL ARGDGAIYLR FPHKGYREKI WDHAAGSIVV
     TEAGGLVTDA SGNDLDFSKG RFLDLDTGII ATNKQLMPSL LKAVQDAIKE QNQAASPL
 
 
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