ID W9VUW0_9EURO Unreviewed; 355 AA.
AC W9VUW0;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-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=A1O5_12214 {ECO:0000313|EMBL:EXJ59333.1};
OS Cladophialophora psammophila CBS 110553.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae;
OC Cladophialophora.
OX NCBI_TaxID=1182543 {ECO:0000313|EMBL:EXJ59333.1, ECO:0000313|Proteomes:UP000019471};
RN [1] {ECO:0000313|EMBL:EXJ59333.1, ECO:0000313|Proteomes:UP000019471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 110553 {ECO:0000313|EMBL:EXJ59333.1,
RC ECO:0000313|Proteomes:UP000019471};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Cladophialophora psammophila CBS 110553.";
RL Submitted (MAR-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}.
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:EXJ59333.1}.
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DR EMBL; AMGX01000032; EXJ59333.1; -; Genomic_DNA.
DR RefSeq; XP_007750973.1; XM_007752783.1.
DR AlphaFoldDB; W9VUW0; -.
DR STRING; 1182543.W9VUW0; -.
DR GeneID; 19196900; -.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_1_1_1; -.
DR OrthoDB; 5486961at2759; -.
DR Proteomes; UP000019471; 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; 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; PS00630; IMP_2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019471}.
SQ SEQUENCE 355 AA; 37899 MW; 21F592805F11331C CRC64;
MSSQYAHEHQ IALLAVQRAT VLTQEVYNST FKGTVSKSDA SPVTIADFGA QALITSAILH
NFPQDTIVAE EEASKLREHE SLRNQLWHCV QNVRLDDEIA EETLGGPVAT IEILLDAIDR
GKGQGGNTGR VWAIDPVDGT KGLLRGGQYA IALALIVDGD VQVGVLGCPN LPVDDSVRLD
AKIGFNQSGG VGSGVLISAE KGQGASSRRL TKGRLAPAHQ VGMRPVRYVS NAILCEAVEP
TFSNHAQQNA VARALEITKV VRLDSQAKYA SLARGAADIL LRLPVRKDYE ENIWDHAAGD
LIVREAGGII TDVFGKPLNF GVGRKLKENS GFVCAPQGIH AKVLAAVQDV LAIRP
//
