ID   S7ZYC3_PENO1            Unreviewed;       352 AA.
AC   S7ZYC3;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=PDE_08758 {ECO:0000313|EMBL:EPS33796.1};
OS   Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS33796.1, ECO:0000313|Proteomes:UP000019376};
RN   [1] {ECO:0000313|EMBL:EPS33796.1, ECO:0000313|Proteomes:UP000019376}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX   PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA   Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA   Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT   "Genomic and secretomic analyses reveal unique features of the
RT   lignocellulolytic enzyme system of Penicillium decumbens.";
RL   PLoS ONE 8:E55185-E55185(2013).
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; KB644415; EPS33796.1; -; Genomic_DNA.
DR   AlphaFoldDB; S7ZYC3; -.
DR   STRING; 933388.S7ZYC3; -.
DR   eggNOG; KOG1528; Eukaryota.
DR   HOGENOM; CLU_033446_1_1_1; -.
DR   OrthoDB; 5486961at2759; -.
DR   PhylomeDB; S7ZYC3; -.
DR   Proteomes; UP000019376; 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:UP000019376}.
SQ   SEQUENCE   352 AA;  37117 MW;  A9A0680DDF5BDBBC CRC64;
     MAYQQERYIA ELAVQRATLL TQKVFFEKAK GTVSKDDKSP VTIGDFGAQA LIIQAIRKNF
     PNDEIVAEEE ASTLREDKNL SAEIWRLVQD IKLDDAESDK ILGGPLASEE SMLDIIDAGK
     SAGGAKGRIW ALDPIDGTKG FLRGGQYAVC LGLIVDGDVK VGAIGTPNLP VDDAAPIDAS
     IGAQPSGTSS NGVLFSAVLG EGATSRPLTS GALAQSKSIS MRPVPDIAQA VFCEGVEAAH
     SAQGDNAAVA ERLGITAPSV RLDSQAKYCS IARGAGDIYL RLPVKKDYQE KIWDHAAGDI
     IVREAGGQVT DIYGNRLDFS KGRTLAANKG VVAAPKALQD QVIDAVKTVL KL
//