ID   PHYA_ASPOR              Reviewed;         466 AA.
AC   Q9C1T1; Q2UGV7;
DT   06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Phytase A {ECO:0000303|Ref.1};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:P34752};
DE            EC=3.1.3.8 {ECO:0000269|Ref.1};
DE   AltName: Full=Histidine acid phosphatase phyA {ECO:0000250|UniProtKB:P34752};
DE            Short=HAP {ECO:0000250|UniProtKB:P34752};
DE   AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A {ECO:0000250|UniProtKB:P34752};
DE   AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A {ECO:0000250|UniProtKB:P34752};
DE   Flags: Precursor;
GN   Name=phyA; ORFNames=AO090023000692;
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Gomi K.;
RT   "Nucleotide sequence of Aspergillus oryzae phytase cDNA.";
RL   Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40;
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOTECHNOLOGY.
RX   PubMed=36763800; DOI=10.1093/lambio/ovac077;
RA   Pragya A., Sharma K.K., Kumar S., Manisha P., Singh D., Kumar V., Singh B.;
RT   "Enhanced production and immobilization of phytase from Aspergillus oryzae:
RT   a safe and ideal food supplement for improving nutrition.";
RL   Lett. Appl. Microbiol. 76:0-0(2023).
CC   -!- FUNCTION: Catalyzes the phosphate monoester hydrolysis of phytic acid
CC       (myo-inositol hexakisphosphate), which results in the stepwise
CC       formation of myo-inositol pentakis-, tetrakis-, tris-, bis-, and
CC       monophosphates, as well as the liberation of inorganic phosphate
CC       (PubMed:36763800). Myo-inositol 2-monophosphate is the end product (By
CC       similarity). {ECO:0000250|UniProtKB:P34752,
CC       ECO:0000269|PubMed:36763800}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol hexakisphosphate + H2O = 1D-myo-inositol
CC         1,2,4,5,6-pentakisphosphate + phosphate; Xref=Rhea:RHEA:16989,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:58130; EC=3.1.3.8;
CC         Evidence={ECO:0000269|PubMed:36763800};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000269|PubMed:36763800};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,4,5,6-pentakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,5,6-tetrakisphosphate + phosphate; Xref=Rhea:RHEA:77115,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:57798,
CC         ChEBI:CHEBI:195535; Evidence={ECO:0000250|UniProtKB:P34752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC         Evidence={ECO:0000250|UniProtKB:P34752};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,5,6-tetrakisphosphate + H2O = 1D-myo-
CC         inositol 1,2,6-trisphosphate + phosphate; Xref=Rhea:RHEA:77119,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195535,
CC         ChEBI:CHEBI:195537; Evidence={ECO:0000250|UniProtKB:P34752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC         Evidence={ECO:0000250|UniProtKB:P34752};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2,6-trisphosphate + H2O = 1D-myo-inositol
CC         1,2-bisphosphate + phosphate; Xref=Rhea:RHEA:77131,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:43474, ChEBI:CHEBI:195537,
CC         ChEBI:CHEBI:195539; Evidence={ECO:0000250|UniProtKB:P34752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC         Evidence={ECO:0000250|UniProtKB:P34752};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1D-myo-inositol 1,2-bisphosphate + H2O = 1D-myo-inositol 2-
CC         phosphate + phosphate; Xref=Rhea:RHEA:77135, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:84142, ChEBI:CHEBI:195539;
CC         Evidence={ECO:0000250|UniProtKB:P34752};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC         Evidence={ECO:0000250|UniProtKB:P34752};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O00085}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- BIOTECHNOLOGY: Phytic acid is the major storage form of phosphorus in
CC       plant seeds and, thus, in seed-based animal feed. Phytases are
CC       therefore of considerable economic interest.
CC       {ECO:0000269|PubMed:36763800}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; AB042805; BAB40715.1; -; mRNA.
DR   EMBL; AP007157; BAE59208.1; -; Genomic_DNA.
DR   RefSeq; XP_001821210.1; XM_001821158.2.
DR   AlphaFoldDB; Q9C1T1; -.
DR   SMR; Q9C1T1; -.
DR   STRING; 510516.Q9C1T1; -.
DR   GlyCosmos; Q9C1T1; 7 sites, No reported glycans.
DR   EnsemblFungi; BAE59208; BAE59208; AO090023000692.
DR   GeneID; 5993212; -.
DR   KEGG; aor:AO090023000692; -.
DR   HOGENOM; CLU_020880_0_0_1; -.
DR   OrthoDB; 2721627at2759; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR000560; His_Pase_clade-2.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   InterPro; IPR016274; Histidine_acid_Pase_euk.
DR   PANTHER; PTHR20963:SF24; 3-PHYTASE B; 1.
DR   PANTHER; PTHR20963; MULTIPLE INOSITOL POLYPHOSPHATE PHOSPHATASE-RELATED; 1.
DR   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
DR   PROSITE; PS00778; HIS_ACID_PHOSPHAT_2; 1.
PE   1: Evidence at protein level;
KW   Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..466
FT                   /note="Phytase A"
FT                   /id="PRO_0000043346"
FT   ACT_SITE        81
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   BINDING         49
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         50
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         80
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         81
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         84
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         87
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         164
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         300
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         360
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         361
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   CARBOHYD        104
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        119
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        206
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        219
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        338
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        351
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        375
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        30..39
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        70..413
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        214..464
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        263..281
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        435..443
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
SQ   SEQUENCE   466 AA;  51257 MW;  8033BED57FBA2791 CRC64;
     MAVLSVLLPI TFLLSSVTGT PVTSPRQQSC NTVDEGYQCF SGVSHLWGQY SPYFSVDDES
     SLSEDVPDHC QVTFAQVLSR HGARYPTKSK SEKYAKLIKA VQHNATSFSG KYAFLKSYNY
     SLGADDLTPF GENQLVDSGI KFYQRYEELA KNVVPFIRAS GSDRVIASGE KFIEGFQKAK
     LGDSKSKRGQ PAPIVNVVIT ETEGFNNTLD HSLCTAFENS TTGDDAEDKF TAVFTPSIVE
     RLEKDLPGTT LSSKEVVYLM DMCSFDTIAL TRDGSRLSPF CALFTQEEWA QYDYLQSVSK
     YYGYGGGNPL GPAQGIGFAN ELIARLTKSP VKDHTTTNTT LDSNPATFPL NATLYADFSH
     DNTMTSVFFA LGLYNTTEPL SQTSVQSTEE TNGYSSARTV PFGARAYVEM MQCTDEKEPL
     VRVLVNDRVI PLQGCDADEY GRCKRDDFVE GLSFVTSGGN WGECFA
//