ID E3KGV0_PUCGT Unreviewed; 427 AA.
AC E3KGV0;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 58.
DE RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633};
DE EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
GN ORFNames=PGTG_08711 {ECO:0000313|EMBL:EFP83525.1};
OS Puccinia graminis f. sp. tritici (strain CRL 75-36-700-3 / race SCCL)
OS (Black stem rust fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC Pucciniomycetes; Pucciniales; Pucciniaceae; Puccinia.
OX NCBI_TaxID=418459 {ECO:0000313|EMBL:EFP83525.1, ECO:0000313|Proteomes:UP000008783};
RN [1]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3;
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (JAN-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EFP83525.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CRL 75-36-700-3 {ECO:0000313|EMBL:EFP83525.1};
RG The Broad Institute Genome Sequencing Platform;
RA Birren B., Lander E., Galagan J., Nusbaum C., Devon K., Cuomo C., Jaffe D.,
RA Butler J., Alvarez P., Gnerre S., Grabherr M., Mauceli E., Brockman W.,
RA Young S., LaButti K., Sykes S., DeCaprio D., Crawford M., Koehrsen M.,
RA Engels R., Montgomery P., Pearson M., Howarth C., Larson L., White J.,
RA Zeng Q., Kodira C., Yandava C., Alvarado L., O'Leary S., Szabo L., Dean R.,
RA Schein J.;
RT "The Genome Sequence of Puccinia graminis f. sp. tritici Strain CRL 75-36-
RT 700-3.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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 -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC {ECO:0000256|ARBA:ARBA00009759}.
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DR EMBL; DS178286; EFP83525.1; -; Genomic_DNA.
DR RefSeq; XP_003327944.1; XM_003327896.2.
DR AlphaFoldDB; E3KGV0; -.
DR STRING; 418459.E3KGV0; -.
DR EnsemblFungi; EFP83525; EFP83525; PGTG_08711.
DR GeneID; 10532206; -.
DR KEGG; pgr:PGTG_08711; -.
DR VEuPathDB; FungiDB:PGTG_08711; -.
DR eggNOG; KOG1528; Eukaryota.
DR HOGENOM; CLU_033446_1_1_1; -.
DR InParanoid; E3KGV0; -.
DR OMA; MSYQQER; -.
DR OrthoDB; 5486961at2759; -.
DR Proteomes; UP000008783; Unassembled WGS sequence.
DR GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046854; P:phosphatidylinositol phosphate biosynthetic process; IEA:InterPro.
DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central.
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};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000008783}.
SQ SEQUENCE 427 AA; 46896 MW; 9D9B9E6878F16A6B CRC64;
MPAAFQIQRI GISSSRLFGC SRTLHSKPIP QLLDQRNSTK AMVIPIQSGY QLEREVAVAA
VLQASLVTRR IFDKLIRPGL QTGDNNQASI TKVDRSPVTV GDYTVQALLN FILSKYFPDD
EIVGEEDSSE LLKTTDKKHL QQIIDFTNEG LKEDRLSIPT DEEKWSKFRS QPALTEDELV
KLIDLGKSAG GKPGENRRFW TLDPIDGTKG FLRGGQYAIC LALIVDGEAV LGVIGTPNLP
LKGIPSPTDT EPTGVLFLAE KGSGAFQRAL GVDEYTEIKM KPHERGSLGR EGTFCESFDA
GHSNQLVTGD IARKLNMLNA QSPIRIDSQA KYCVLARGDS DVYLRFPTQA DYQEKIWDHA
AGSIIISEAG GKVVDLDGKP LDFSGGRTLS NNHPGFLACH NQVLVDVLKA AKAAHENQLK
QQKLHKY
//
