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Database: UniProt
Entry: E9DYN2_METAQ
LinkDB: E9DYN2_METAQ
Original site: E9DYN2_METAQ 
ID   E9DYN2_METAQ            Unreviewed;       358 AA.
AC   E9DYN2;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   05-APR-2011, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=MAC_02729 {ECO:0000313|EMBL:EFY91302.1};
OS   Metarhizium acridum (strain CQMa 102).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Metarhizium.
OX   NCBI_TaxID=655827 {ECO:0000313|Proteomes:UP000002499};
RN   [1] {ECO:0000313|EMBL:EFY91302.1, ECO:0000313|Proteomes:UP000002499}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQMa 102 {ECO:0000313|EMBL:EFY91302.1,
RC   ECO:0000313|Proteomes:UP000002499};
RX   PubMed=21253567; DOI=10.1371/journal.pgen.1001264;
RA   Gao Q., Jin K., Ying S.H., Zhang Y., Xiao G., Shang Y., Duan Z., Hu X.,
RA   Xie X.Q., Zhou G., Peng G., Luo Z., Huang W., Wang B., Fang W., Wang S.,
RA   Zhong Y., Ma L.J., St Leger R.J., Zhao G.P., Pei Y., Feng M.G., Xia Y.,
RA   Wang C.;
RT   "Genome sequencing and comparative transcriptomics of the model
RT   entomopathogenic fungi Metarhizium anisopliae and M. acridum.";
RL   PLoS Genet. 7:E1001264-E1001264(2011).
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; GL698483; EFY91302.1; -; Genomic_DNA.
DR   RefSeq; XP_007809069.1; XM_007810878.1.
DR   AlphaFoldDB; E9DYN2; -.
DR   STRING; 655827.E9DYN2; -.
DR   GeneID; 19247040; -.
DR   KEGG; maw:MAC_02729; -.
DR   eggNOG; KOG1528; Eukaryota.
DR   HOGENOM; CLU_033446_1_1_1; -.
DR   InParanoid; E9DYN2; -.
DR   OMA; MSYQQER; -.
DR   OrthoDB; 5486961at2759; -.
DR   Proteomes; UP000002499; 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   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:UP000002499}.
SQ   SEQUENCE   358 AA;  38373 MW;  8A51B623D711C4AF CRC64;
     MVTAPSYSHE LEVAQLAVQR ATILTKRVFH EKAKGTVDKN DKSPVTIGDF GAQALIIAAL
     KHNFPGDAIV AEEEAVQLKE DANLRQTIWD LVKDTKLDDD KAEQTLGGGI KSVDSMLELI
     DLGNSPGGSK GRIWTIDPID GTKGFLRGGQ YAVCLGLMVD GEVRVGVLGC PNLPVDDSAR
     LTADIGSNAT DEGRGVIFYA VEHKGAGSRP LTTGGLSPDS KHIGMRPIED LSRATFCESV
     EAGHSSHDDQ AIISQKLGIT EPSVRMDSQA KYGSIARGAG DIYLRLPVKA SYQEKIWDHA
     AGDLIVRESG GQVTDIYGKR LDFSVGRTLA NNKGVVAAPL GVHERVLRVV QEVLKIEQ
//
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