ID A0A100ITS2_ASPNG Unreviewed; 366 AA.
AC A0A100ITS2;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
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=ABL_09864 {ECO:0000313|EMBL:GAQ47203.1};
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ47203.1, ECO:0000313|Proteomes:UP000068243};
RN [1] {ECO:0000313|Proteomes:UP000068243}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT "Draft genome sequence of Aspergillus niger strain An76.";
RL Genome Announc. 4:E0170015-E0170015(2016).
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GAQ47203.1}.
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DR EMBL; BCMY01000026; GAQ47203.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A100ITS2; -.
DR VEuPathDB; FungiDB:An05g00490; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1157134; -.
DR VEuPathDB; FungiDB:ATCC64974_38790; -.
DR VEuPathDB; FungiDB:M747DRAFT_283958; -.
DR OMA; WSSHVRY; -.
DR Proteomes; UP000068243; 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: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; IPR000760; Inositol_monophosphatase-like.
DR NCBIfam; TIGR01330; bisphos_HAL2; 1.
DR PANTHER; PTHR43200:SF2; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU368076};
KW Magnesium {ECO:0000256|RuleBase:RU368076};
KW Metal-binding {ECO:0000256|RuleBase:RU368076}.
SQ SEQUENCE 366 AA; 40273 MW; 0850C55EAF084254 CRC64;
MAHSPFAREL QVACLAVQRA SIVTKTMLAE ADKGSTDKAD ASPVTIADFA SQAILISAIR
HNFPSDKFVG EESASALRND PALADRVWQL VSTTQLHDTE SEEIVAAPSS LEEMLSIIDL
GGSGEGARHT RTWIMDPIDG TASFIQGRQY AVSVALIENG EQKVGVVGYP NLHFHTTVVH
EDTVDQNGYG IMLSAVRGHG AYKRPMSKER LQPAVKVYNV LARTDTGQPD LVFAESMESP
YIDQRLHQVV RERLGVTKPI TDLWSMQAKY AALVVGGCNV MVRIPRSPEY RAYAWDHAGG
MLVFEESGGM ITDLDGQPFN YGRGRTLADN LGLVAAFPEI HSRVLELARE IRERHKEEVM
KDNTQQ
//
