ID   PHYA_EMENI              Reviewed;         463 AA.
AC   O00093; C8VNT4; Q5BCP5;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2007, sequence version 2.
DT   27-MAR-2024, entry version 121.
DE   RecName: Full=Phytase A {ECO:0000303|PubMed:9349716};
DE            EC=3.1.3.- {ECO:0000269|PubMed:9925555};
DE            EC=3.1.3.8 {ECO:0000269|PubMed:9349716, ECO:0000269|PubMed:9925555};
DE   AltName: Full=Histidine acid phosphatase phyA {ECO:0000303|PubMed:9349716};
DE            Short=HAP {ECO:0000303|PubMed:9349716};
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|PubMed:9349716}; ORFNames=AN1685;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], CLEAVAGE, AND CATALYTIC ACTIVITY.
RX   PubMed=9349716; DOI=10.1016/s0167-4781(97)00107-3;
RA   Pasamontes L., Haiker M., Henriquez-Huecas M., Mitchell D.B.,
RA   van Loon A.P.G.M.;
RT   "Cloning of the phytases from Emericella nidulans and the thermophilic
RT   fungus Talaromyces thermophilus.";
RL   Biochim. Biophys. Acta 1353:217-223(1997).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [4]
RP   FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP   BIOTECHNOLOGY.
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:9349716, PubMed:9925555). Myo-inositol 2-monophosphate is the
CC       end product (PubMed:9925555). Has a broad substrate specificity and is
CC       also able to dephosphorylate other classic acid phosphatase substrates
CC       such as p-nitrophenyl phosphate, phenyl phosphate, fructose 1,6-
CC       bisphosphate, fructose 6-phosphate, glucose 6-phosphate, ribose 5-
CC       phosphate, alpha-glycerophosphate, beta-glycerophosphate, 3-
CC       phosphoglycerate, as well as ADP and ATP (PubMed:9925555).
CC       {ECO:0000269|PubMed:9349716, 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:9349716,
CC         ECO:0000269|PubMed:9925555};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC         Evidence={ECO:0000269|PubMed:9349716, 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       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:9925555};
CC   -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:O00085}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- PTM: Seems to be cleaved into at least two pieces, most likely due to
CC       proteases in the supernatant. The N-terminal fragment, called phyB
CC       seems to retain phytase activity. {ECO:0000269|PubMed:9349716}.
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:9925555}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; U59803; AAB96871.1; -; Genomic_DNA.
DR   EMBL; AACD01000026; EAA64805.1; -; Genomic_DNA.
DR   EMBL; BN001307; CBF85365.1; -; Genomic_DNA.
DR   RefSeq; XP_659289.1; XM_654197.1.
DR   AlphaFoldDB; O00093; -.
DR   SMR; O00093; -.
DR   STRING; 227321.O00093; -.
DR   GlyCosmos; O00093; 9 sites, No reported glycans.
DR   EnsemblFungi; CBF85365; CBF85365; ANIA_01685.
DR   GeneID; 2874708; -.
DR   KEGG; ani:AN1685.2; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_0_0_1; -.
DR   InParanoid; O00093; -.
DR   OMA; CRVTFAQ; -.
DR   OrthoDB; 2721627at2759; -.
DR   BRENDA; 3.1.3.26; 517.
DR   BRENDA; 3.1.3.8; 517.
DR   Proteomes; UP000000560; Chromosome VII.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003993; F:acid phosphatase activity; IBA:GO_Central.
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..463
FT                   /note="Phytase A"
FT                   /id="PRO_0000023976"
FT   ACT_SITE        80
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   BINDING         48
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         49
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         79
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         83
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         86
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         163
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         207
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         297
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         357
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   BINDING         358
FT                   /ligand="1D-myo-inositol hexakisphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58130"
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   CARBOHYD        26
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        41
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        103
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        118
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        203
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        226
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        331
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        335
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        372
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        29..38
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        69..410
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        211..460
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        260..278
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   DISULFID        431..439
FT                   /evidence="ECO:0000250|UniProtKB:O00092"
FT   CONFLICT        19
FT                   /note="T -> A (in Ref. 1; AAB96871)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   463 AA;  51816 MW;  1D6BC0B0DA14F0D9 CRC64;
     MAFFTVALSL YYLLSRVSTQ APVVQNHSCN TADGGYQCFP NVSHVWGQYS PYFSIEQESA
     ISEDVPHGCE VTFVQVLSRH GARYPTESKS KAYSGLIEAI QKNATSFWGQ YAFLESYNYT
     LGADDLTIFG ENQMVDSGAK FYRRYKNLAR KNTPFIRASG SDRVVASAEK FINGFRKAQL
     HDHGSKRATP VVNVIIPEID GFNNTLDHST CVSFENDERA DEIEANFTAI MGPPIRKRLE
     NDLPGIKLTN ENVIYLMDMC SFDTMARTAH GTELSPFCAI FTEKEWLQYD YLQSLSKYYG
     YGAGSPLGPA QGIGFTNELI ARLTQSPVQD NTSTNHTLDS NPATFPLDRK LYADFSHDNS
     MISIFFAMGL YNGTQPLSMD SVESIQEMDG YAASWTVPFG ARAYFELMQC EKKEPLVRVL
     VNDRVVPLHG CAVDKFGRCT LDDWVEGLNF ARSGGNWKTC FTL
//