ID X0BXY9_FUSOX Unreviewed; 354 AA.
AC X0BXY9;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE SubName: Full=3'(2'),5'-bisphosphate nucleotidase {ECO:0000313|EMBL:EXK83768.1};
GN ORFNames=FOQG_11929 {ECO:0000313|EMBL:EXK83768.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK83768.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK83768.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK83768.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; JH658399; EXK83768.1; -; Genomic_DNA.
DR AlphaFoldDB; X0BXY9; -.
DR HOGENOM; CLU_033446_1_1_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; IPR020583; Inositol_monoP_metal-BS.
DR InterPro; IPR000760; Inositol_monophosphatase-like.
DR PANTHER; PTHR43200:SF2; 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.
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:UP000030663}.
SQ SEQUENCE 354 AA; 38050 MW; 19A6A4E87E57D2F2 CRC64;
MTPFARELHI AQLAVLRASI LTKSVQSRVH EISKDDDSPV TIADFAAQAL LIIALRDAFP
SDKFLGEEDS AALRADEALC SKVFELVSSV ADTIDPNTGI PLPKPSSVAE MLSLIELGGR
GTGGDEGRFW VMDPVDGTAT FLRGQQYAVA LSLIEQGREV IGVLGYPNIS TGMTQISEEN
IDKSGMGIML TAVRGQGSMA RTMTPSGLKD AFPLSIMKTH SNNNNNNNNL HIVDCALSDV
SRHDVIAELA DEFKAKFPNI EVWSSHVRYA ALIVGGGNAQ FWVPASSASK MHIWDHAGAQ
LIFTELGGKV TDLDGKAMDF GAGRDLNRNR GLVVAQGEMH DALLAAMNRI IEGY
//