(data stored in ACNUC27125 zone)

SWISSPROT: Q4WSU4_ASPFU

ID   Q4WSU4_ASPFU            Unreviewed;       330 AA.
AC   Q4WSU4;
DT   05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2005, sequence version 1.
DT   11-DEC-2019, entry version 69.
DE   RecName: Full=Inositol-1-monophosphatase {ECO:0000256|RuleBase:RU364068};
DE            EC=3.1.3.25 {ECO:0000256|RuleBase:RU364068};
GN   ORFNames=AFUA_1G11600 {ECO:0000313|EMBL:EAL90488.1};
OS   Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS   A1100) (Aspergillus fumigatus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL90488.1, ECO:0000313|Proteomes:UP000002530};
RN   [1] {ECO:0000313|EMBL:EAL90488.1, ECO:0000313|Proteomes:UP000002530}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC   {ECO:0000313|Proteomes:UP000002530};
RX   PubMed=16372009; DOI=10.1038/nature04332;
RA   Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA   Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA   Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA   Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA   Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA   Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA   Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA   Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA   Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA   Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA   Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA   Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA   Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA   Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA   Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA   Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA   Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA   Denning D.W.;
RT   "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT   Aspergillus fumigatus.";
RL   Nature 438:1151-1156(2005).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a myo-inositol phosphate + H2O = myo-inositol + phosphate;
CC         Xref=Rhea:RHEA:24056, ChEBI:CHEBI:15377, ChEBI:CHEBI:17268,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84139; EC=3.1.3.25;
CC         Evidence={ECO:0000256|RuleBase:RU364068};
CC   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|RuleBase:RU364068};
CC   -!- PATHWAY: Polyol metabolism; myo-inositol biosynthesis; myo-inositol
CC       from D-glucose 6-phosphate: step 2/2. {ECO:0000256|RuleBase:RU364068}.
CC   -!- SIMILARITY: Belongs to the inositol monophosphatase superfamily.
CC       {ECO:0000256|RuleBase:RU364068}.
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:EAL90488.1}.
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DR   EMBL; AAHF01000004; EAL90488.1; -; Genomic_DNA.
DR   RefSeq; XP_752526.1; XM_747433.1.
DR   STRING; 746128.CADAFUBP00001084; -.
DR   EnsemblFungi; EAL90488; EAL90488; AFUA_1G11600.
DR   GeneID; 3510175; -.
DR   KEGG; afm:AFUA_1G11600; -.
DR   EuPathDB; FungiDB:Afu1g11600; -.
DR   HOGENOM; HOG000282238; -.
DR   InParanoid; Q4WSU4; -.
DR   KO; K01092; -.
DR   OMA; HLFPMFC; -.
DR   OrthoDB; 915621at2759; -.
DR   UniPathway; UPA00823; UER00788.
DR   Proteomes; UP000002530; Chromosome 1.
DR   GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IBA:GO_Central.
DR   GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006021; P:inositol biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046855; P:inositol phosphate dephosphorylation; IBA:GO_Central.
DR   GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IBA:GO_Central.
DR   CDD; cd01639; IMPase; 1.
DR   InterPro; IPR033942; IMPase.
DR   InterPro; IPR020583; Inositol_monoP_metal-BS.
DR   InterPro; IPR000760; Inositol_monophosphatase-like.
DR   InterPro; IPR020550; Inositol_monophosphatase_CS.
DR   Pfam; PF00459; Inositol_P; 1.
DR   PRINTS; PR00377; IMPHPHTASES.
DR   PROSITE; PS00629; IMP_1; 1.
DR   PROSITE; PS00630; IMP_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q4WSU4.
DR   SWISS-2DPAGE; Q4WSU4.
KW   Hydrolase {ECO:0000256|RuleBase:RU364068};
KW   Magnesium {ECO:0000256|RuleBase:RU364068};
KW   Metal-binding {ECO:0000256|RuleBase:RU364068};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002530}.
SQ   SEQUENCE   330 AA;  36588 MW;  2E14AB5C4220EA92 CRC64;
     MAIEFTQDTL DEIYAFAVAL GRRAGDLLLE RIDKQIASDG ETAYTYTEKD NAVDIVTQTD
     EDVETFIKTA IEKRYPEHKF LGEETYAQGQ SRSYLIDAHP TWCIDPLDGT VNFTHLFPTF
     CVSIGFLVNH RPVIGVIYAP AMNQMFSSCV GRGAWLNDTR GARRLPLRRN PIPPMPATSP
     RGCIFACEWG KDRRDIPGGN MARKVESFVR MASESGGMVH GVRSLGSAAL DLAYTAMGAV
     DIWWEGGCWE WDVAAGIAIL REAGGLVTTA NPPANPETDP IEEARLGSRL YLAIRPAGPS
     ETETGRQTQE RTVREVWKRV RELDYTRPGA
//

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