ID   A0A0D2DM75_9EURO        Unreviewed;       357 AA.
AC   A0A0D2DM75;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 31.
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=Z517_08645 {ECO:0000313|EMBL:KIW78806.1};
OS   Fonsecaea pedrosoi CBS 271.37.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Fonsecaea.
OX   NCBI_TaxID=1442368 {ECO:0000313|EMBL:KIW78806.1, ECO:0000313|Proteomes:UP000053029};
RN   [1] {ECO:0000313|EMBL:KIW78806.1, ECO:0000313|Proteomes:UP000053029}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 271.37 {ECO:0000313|EMBL:KIW78806.1,
RC   ECO:0000313|Proteomes:UP000053029};
RG   The Broad Institute Genomics Platform;
RA   Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA   Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA   Birren B.;
RT   "The Genome Sequence of Fonsecaea pedrosoi CBS 271.37.";
RL   Submitted (JAN-2015) 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|ARBA:ARBA00001625,
CC         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; KN846973; KIW78806.1; -; Genomic_DNA.
DR   RefSeq; XP_013282614.1; XM_013427160.1.
DR   AlphaFoldDB; A0A0D2DM75; -.
DR   STRING; 1442368.A0A0D2DM75; -.
DR   GeneID; 25308135; -.
DR   VEuPathDB; FungiDB:Z517_08645; -.
DR   HOGENOM; CLU_033446_1_1_1; -.
DR   OrthoDB; 5486961at2759; -.
DR   Proteomes; UP000053029; 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:SF6; 3'(2'),5'-BISPHOSPHATE NUCLEOTIDASE; 1.
DR   PANTHER; PTHR43200; PHOSPHATASE; 1.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
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:UP000053029}.
SQ   SEQUENCE   357 AA;  37597 MW;  88784F0577C4DF8C CRC64;
     MAPTKEYEHE LKVAQLAVAR AAILTKAVFH EKAKGTVSKD DKSPVTIGDF GAQALIIAAI
     KHNFPNDEVV GEEEASSLRE QKDLSSKIWN LVKDVRLDDP SIDAVLGGPL KSEEAMLDAI
     DQGNSAGGNK GRIWALDPID GTKGFLRGGQ YAVCLALMVD GDVKVGVLGC PNLPVDDSAP
     LTEDIGAAAT DAEGKGVLFS AVQGQGATSQ PLTRGLPTNG QPIHVSKISK VSEAVMCESV
     EPGHSSKGDN ALIAEKLGIT GRPVQMDSQA KYGSVARGAG DLYLRLPVRK DYIEKIWDHA
     AGDLIVREAG GQVTDVTGKR LNFSLGRTLL ENKGVIATPA NVHAEVLKAV QEVLAAK
//