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Database: UniProt
Entry: W9QI47_9ROSA
LinkDB: W9QI47_9ROSA
Original site: W9QI47_9ROSA 
ID   W9QI47_9ROSA            Unreviewed;       382 AA.
AC   W9QI47;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633, ECO:0000256|RuleBase:RU368076};
DE            EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633, ECO:0000256|RuleBase:RU368076};
GN   ORFNames=L484_010200 {ECO:0000313|EMBL:EXB37726.1};
OS   Morus notabilis.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Rosales; Moraceae; Moreae; Morus.
OX   NCBI_TaxID=981085 {ECO:0000313|EMBL:EXB37726.1, ECO:0000313|Proteomes:UP000030645};
RN   [1] {ECO:0000313|Proteomes:UP000030645}
RP   NUCLEOTIDE SEQUENCE.
RA   He N., Zhao S.;
RT   "Draft Genome Sequence of a Mulberry Tree, Morus notabilis C.K. Schneid.";
RL   Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU368076}.
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         Evidence={ECO:0000256|RuleBase:RU368076};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946,
CC         ECO:0000256|RuleBase:RU368076};
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|ARBA:ARBA00009759, ECO:0000256|RuleBase:RU368076}.
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DR   EMBL; KE343656; EXB37726.1; -; Genomic_DNA.
DR   RefSeq; XP_010089382.1; XM_010091080.1.
DR   AlphaFoldDB; W9QI47; -.
DR   STRING; 981085.W9QI47; -.
DR   GeneID; 21393503; -.
DR   KEGG; mnt:21393503; -.
DR   eggNOG; KOG1528; Eukaryota.
DR   OrthoDB; 5486961at2759; -.
DR   Proteomes; UP000030645; Unassembled WGS sequence.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043647; P:inositol phosphate metabolic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR   GO; GO:0000103; P:sulfate assimilation; IEA:UniProtKB-UniRule.
DR   CDD; cd01517; PAP_phosphatase; 1.
DR   Gene3D; 3.40.190.80; -; 1.
DR   Gene3D; 3.30.540.10; Fructose-1,6-Bisphosphatase, subunit A, domain 1; 1.
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   NCBIfam; TIGR01330; bisphos_HAL2; 1.
DR   PANTHER; PTHR43200:SF24; PAP-SPECIFIC PHOSPHATASE HAL2-LIKE; 1.
DR   PANTHER; PTHR43200; PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   SUPFAM; SSF56655; Carbohydrate phosphatase; 1.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368076};
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU368076};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU368076};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030645}.
SQ   SEQUENCE   382 AA;  41152 MW;  4DC0A969C5641DB9 CRC64;
     MGSENYSKEL DVAVRVVHMA CSLCQRVQDG LVSVEKSEQV KSKDDDSPVT IADWSVQATV
     SWVLSESFGN KNVSIVAEED VKTLSKADSA GLLAAVVNTV NECLAEAPKY GLKPPAKALE
     TSQVLEAIGR CNSTGGPKGR HWVLDPVDGT LGFVRGDQYA VALALIEDGK VVTGVLGCPN
     YPMKKELLNY HYQPHQSMLK FSPPAMNSWG KGCVMYAVKG SGEAWMQSLT HGANKLEWPN
     SAMLIRVSSI DDPALATSCE PVEKTNSNHS FTQGLAHSVG LRKQPLRVHS MVKYAAIARG
     DAEIFMKFAR SGYKEKIWDH AAGVLIVEEA GGVVTDARGH PLDFSKGVYL EGLDRGIVAC
     SGATLHEKII SAVYASWDSS NL
//
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