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Database: UniProt
Entry: F4R422_MELLP
LinkDB: F4R422_MELLP
Original site: F4R422_MELLP 
ID   F4R422_MELLP            Unreviewed;       373 AA.
AC   F4R422;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000256|ARBA:ARBA00012633};
DE            EC=3.1.3.7 {ECO:0000256|ARBA:ARBA00012633};
GN   ORFNames=MELLADRAFT_32223 {ECO:0000313|EMBL:EGG13067.1};
OS   Melampsora larici-populina (strain 98AG31 / pathotype 3-4-7) (Poplar leaf
OS   rust fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Pucciniomycotina;
OC   Pucciniomycetes; Pucciniales; Melampsoraceae; Melampsora.
OX   NCBI_TaxID=747676 {ECO:0000313|Proteomes:UP000001072};
RN   [1] {ECO:0000313|Proteomes:UP000001072}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=98AG31 / pathotype 3-4-7 {ECO:0000313|Proteomes:UP000001072};
RX   PubMed=21536894; DOI=10.1073/pnas.1019315108;
RA   Duplessis S., Cuomo C.A., Lin Y.-C., Aerts A., Tisserant E.,
RA   Veneault-Fourrey C., Joly D.L., Hacquard S., Amselem J., Cantarel B.L.,
RA   Chiu R., Coutinho P.M., Feau N., Field M., Frey P., Gelhaye E.,
RA   Goldberg J., Grabherr M.G., Kodira C.D., Kohler A., Kuees U.,
RA   Lindquist E.A., Lucas S.M., Mago R., Mauceli E., Morin E., Murat C.,
RA   Pangilinan J.L., Park R., Pearson M., Quesneville H., Rouhier N.,
RA   Sakthikumar S., Salamov A.A., Schmutz J., Selles B., Shapiro H.,
RA   Tanguay P., Tuskan G.A., Henrissat B., Van de Peer Y., Rouze P.,
RA   Ellis J.G., Dodds P.N., Schein J.E., Zhong S., Hamelin R.C.,
RA   Grigoriev I.V., Szabo L.J., Martin F.;
RT   "Obligate biotrophy features unraveled by the genomic analysis of rust
RT   fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:9166-9171(2011).
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; GL883090; EGG13067.1; -; Genomic_DNA.
DR   RefSeq; XP_007404005.1; XM_007403943.1.
DR   AlphaFoldDB; F4R422; -.
DR   STRING; 747676.F4R422; -.
DR   EnsemblFungi; EGG13067; EGG13067; MELLADRAFT_32223.
DR   GeneID; 18927182; -.
DR   KEGG; mlr:MELLADRAFT_32223; -.
DR   VEuPathDB; FungiDB:MELLADRAFT_32223; -.
DR   eggNOG; KOG1528; Eukaryota.
DR   HOGENOM; CLU_033446_2_1_1; -.
DR   InParanoid; F4R422; -.
DR   OrthoDB; 5486961at2759; -.
DR   Proteomes; UP000001072; Unassembled WGS sequence.
DR   GO; GO:0008441; F:3'(2'),5'-bisphosphate nucleotidase activity; IEA:UniProtKB-EC.
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:0006790; P:sulfur compound metabolic process; IEA:InterPro.
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:UP000001072}.
SQ   SEQUENCE   373 AA;  41751 MW;  5C3EF97CCC32AE05 CRC64;
     MLKLNEIKTN FQKERQIGIS SILKSTILTQ KVFKTLIQKD QIITKQDKSP VTIGDYGSQA
     LINLLISKHF PNDKIIGEEE IQDLQTTSNS PTLNQIERLI NETLTTKLES ETDEEVWKNS
     RIPKSLNQSE ILETINLGNS KEENEDEGNG ERFWTLDPID GTKGFLRSDQ YSICLSLIIN
     KKVTLSFISA PNLSTDPYPS SSNPSSKIGT LFYAEHGKGA YQRPINTNDS SIYSPIRTNP
     ISFNGFQTSG TFCESWESNH SNQILNSKIL AHLKLSNPTP IRLDSQVKYC LIARGDVNVY
     LRLPIDLNYK EKIWDHAAGS LLVEEAGGKV TDMWGKPLDF SLGKTLIQNE GIVASHPNLH
     QSLLDAIKSV SKL
//
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