ID   PHYA_ASPAW              Reviewed;         467 AA.
AC   P34753;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   24-JAN-2024, entry version 91.
DE   RecName: Full=Phytase A {ECO:0000303|PubMed:8224894};
DE            EC=3.1.3.- {ECO:0000250|UniProtKB:P34752};
DE            EC=3.1.3.8 {ECO:0000269|PubMed:8224894};
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; Synonyms=phy {ECO:0000303|PubMed:8224894};
OS   Aspergillus awamori (Black koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=105351;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=ALK0243;
RX   PubMed=8224894; DOI=10.1016/0378-1119(93)90224-q;
RA   Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A.,
RA   Miettinen-Oinonen A., Nevalainen H., Rambosek J.A.;
RT   "The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-
RT   optimum acid phosphatase (aph) from Aspergillus niger var. awamori.";
RL   Gene 133:55-62(1993).
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:8224894). Myo-inositol 2-monophosphate is the end product (By
CC       similarity). {ECO:0000250|UniProtKB:P34752,
CC       ECO:0000269|PubMed:8224894}.
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; Evidence={ECO:0000269|PubMed:8224894};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000269|PubMed:8224894};
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:0000250|UniProtKB:P34752}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; L02421; AAA16898.1; -; Unassigned_DNA.
DR   PIR; JN0889; JN0889.
DR   AlphaFoldDB; P34753; -.
DR   SMR; P34753; -.
DR   GlyCosmos; P34753; 10 sites, No reported glycans.
DR   BRENDA; 3.1.3.26; 494.
DR   BRENDA; 3.1.3.8; 494.
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; Secreted; Signal.
FT   SIGNAL          1..23
FT                   /evidence="ECO:0000255"
FT   CHAIN           24..467
FT                   /note="Phytase A"
FT                   /id="PRO_0000023971"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   BINDING         50
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         51
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         82
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         85
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         88
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         165
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         301
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   BINDING         362
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   CARBOHYD        27
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        59
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        105
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        120
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        207
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        230
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        339
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        352
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        376
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        388
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        31..40
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        71..414
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        215..465
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        264..282
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        436..444
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
SQ   SEQUENCE   467 AA;  51075 MW;  118E828A5D7EC661 CRC64;
     MGVSAVLLPL YLLAGVTSGL AVPASRNQST CDTVDQGYQC FSETSHLWGQ YAPFFSLANE
     SAISPDVPAG CRVTFAQVLS RHGARYPTES KGKKYSALIE EIQQNVTTFD GKYAFLKTYN
     YSLGADDLTP FGEQELVNSG IKFYQRYESL TRNIIPFIRS SGSSRVIASG EKFIEGFQST
     KLKDPRAQPG QSSPKIDVVI SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFAPSIR
     QRLENDLSGV TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW IHYDYLQSLK
     KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSNPATFP LNSTLYADFS
     HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT VPFASRLYVE MMQCQAEQEP
     LVRVLVNDRV VPLHGCPIDA LGRCTRDSFV RGLSFARSGG DWAECSA
//