ID   PHYA2_ASPTE             Reviewed;         466 AA.
AC   O00100;
DT   17-APR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   24-JAN-2024, entry version 86.
DE   RecName: Full=Phytase A {ECO:0000303|PubMed:9925554};
DE            EC=3.1.3.- {ECO:0000269|PubMed:9925555};
DE            EC=3.1.3.8 {ECO:0000269|PubMed:9925555};
DE   AltName: Full=Histidine acid phosphatase phyA {ECO:0000303|PubMed:9925555};
DE            Short=HAP {ECO:0000303|PubMed:9925555};
DE   AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A {ECO:0000303|PubMed:9925555};
DE   AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A {ECO:0000303|PubMed:9925555};
DE   Flags: Precursor;
GN   Name=phyA {ECO:0000303|Ref.1};
OS   Aspergillus terreus.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=33178;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI
RC   44243;
RA   Pasamontes L., Haiker M., Henriquez Huecas M., Hug D., Mitchell D.B.,
RA   Broger C., van Loon A.P.;
RT   "Cloning of the phytases of Aspergillus nidulans and Talaromyces
RT   thermophilus and their evolutionary relation to other histidine acid
RT   phosphatases.";
RL   Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   PROTEIN SEQUENCE OF 20-35, AND SUBUNIT.
RC   STRAIN=ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI
RC   44243;
RX   PubMed=9925554; DOI=10.1128/aem.65.2.359-366.1999;
RA   Wyss M., Pasamontes L., Friedlein A., Remy R., Tessier M., Kronenberger A.,
RA   Middendorf A., Lehmann M., Schnoebelen L., Roethlisberger U., Kusznir E.,
RA   Wahl G., Mueller F., Lahm H.-W., Vogel K., van Loon A.P.G.M.;
RT   "Biophysical characterization of fungal phytases (myo-inositol
RT   hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern,
RT   and engineering of proteolytic resistance.";
RL   Appl. Environ. Microbiol. 65:359-366(1999).
RN   [3]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=9925555; DOI=10.1128/aem.65.2.367-373.1999;
RA   Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt G.,
RA   Lehmann M., van Loon A.P.G.M.;
RT   "Biochemical characterization of fungal phytases (myo-inositol
RT   hexakisphosphate phosphohydrolases): catalytic properties.";
RL   Appl. Environ. Microbiol. 65:367-373(1999).
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:9925555). Myo-inositol 2-monophosphate is the end product
CC       (PubMed:9925555). Has a broad substrate specificity and is also able to
CC       dephosphorylate other classic acid phosphatase substrates such as p-
CC       nitrophenyl phosphate, phenyl phosphate, fructose 1,6-bisphosphate,
CC       glucose 6-phosphate, 3-phosphoglycerate, as well as ADP and ATP
CC       (PubMed:9925555). {ECO:0000269|PubMed:9925555}.
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:9925555};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77116;
CC         Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77120;
CC         Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77132;
CC         Evidence={ECO:0000269|PubMed:9925555};
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:0000269|PubMed:9925555};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:77136;
CC         Evidence={ECO:0000269|PubMed:9925555};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=23.2 uM for phytate {ECO:0000269|PubMed:9925555};
CC       pH dependence:
CC         Optimum pH is 5.5. Active from 4 to 6.5.
CC         {ECO:0000269|PubMed:9925555};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:9925554}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; U60412; AAB58465.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00100; -.
DR   SMR; O00100; -.
DR   GlyCosmos; O00100; 8 sites, No reported glycans.
DR   VEuPathDB; FungiDB:ATEG_05333; -.
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   Direct protein sequencing; Disulfide bond; Glycoprotein; Hydrolase;
KW   Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:9925554"
FT   CHAIN           20..466
FT                   /note="Phytase A"
FT                   /id="PRO_0000283712"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
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        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   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   466 AA;  51055 MW;  F2AECEC1AF7C22C4 CRC64;
     MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL YAPYFSLQDE
     SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA AIQKNATALP GKYAFLKSYN
     YSMGSENLNP FGRNQLQDLG AQFYRRYDTL TRHINPFVRA ADSSRVHESA EKFVEGFQNA
     RQGDPHANPH QPSPRVDVVI PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA
     KRLEADLPGV QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD
     KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP LNATLYADFS
     HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT VPFAARAYIE MMQCRAEKQP
     LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV EGLSFARAGG NWAECF
//