ID PHYA_ARTBC Reviewed; 456 AA.
AC D4ANW6;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=Phytase A {ECO:0000250|UniProtKB:P34752};
DE EC=3.1.3.- {ECO:0000250|UniProtKB:P34752};
DE EC=3.1.3.8 {ECO:0000250|UniProtKB:P34752};
DE AltName: Full=Allergen Asp n 25 homolog {ECO:0000305|PubMed:21919205};
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 ORFNames=ARB_05933;
OS Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS mentagrophytes).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663331;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4681 / CBS 112371;
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND SUBCELLULAR LOCATION.
RX PubMed=21919205; DOI=10.1002/pmic.201100234;
RA Sriranganadane D., Waridel P., Salamin K., Feuermann M., Mignon B.,
RA Staib P., Neuhaus J.M., Quadroni M., Monod M.;
RT "Identification of novel secreted proteases during extracellular
RT proteolysis by dermatophytes at acidic pH.";
RL Proteomics 11:4422-4433(2011).
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 (By
CC similarity). Myo-inositol 2-monophosphate is the end product (By
CC similarity). {ECO:0000250|UniProtKB:P34752}.
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:0000250|UniProtKB:P34752};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:16990;
CC Evidence={ECO:0000250|UniProtKB:P34752};
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:0000269|PubMed:21919205}.
CC -!- ALLERGEN: May cause an allergic reaction in human. {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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ABSU01000004; EFE34977.1; -; Genomic_DNA.
DR RefSeq; XP_003015622.1; XM_003015576.1.
DR AlphaFoldDB; D4ANW6; -.
DR SMR; D4ANW6; -.
DR STRING; 663331.D4ANW6; -.
DR GeneID; 9525903; -.
DR KEGG; abe:ARB_05933; -.
DR eggNOG; KOG1382; Eukaryota.
DR HOGENOM; CLU_020880_0_0_1; -.
DR OMA; CRVTFAQ; -.
DR OrthoDB; 2721627at2759; -.
DR Proteomes; UP000008866; Unassembled WGS sequence.
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 Allergen; Disulfide bond; Glycoprotein; Hydrolase; Reference proteome;
KW Secreted; Signal.
FT SIGNAL 1..24
FT /evidence="ECO:0000255"
FT CHAIN 25..456
FT /note="Phytase A"
FT /evidence="ECO:0000255"
FT /id="PRO_0000434430"
FT ACT_SITE 69
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT BINDING 37
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 38
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 68
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 69
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 72
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 75
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 152
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 283
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 343
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT BINDING 344
FT /ligand="1D-myo-inositol hexakisphosphate"
FT /ligand_id="ChEBI:CHEBI:58130"
FT /evidence="ECO:0000250|UniProtKB:P34752"
FT CARBOHYD 317
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT CARBOHYD 358
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
FT DISULFID 58..396
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 197..450
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 246..264
FT /evidence="ECO:0000250|UniProtKB:O00092"
FT DISULFID 421..429
FT /evidence="ECO:0000250|UniProtKB:O00092"
SQ SEQUENCE 456 AA; 50491 MW; 8ECADBB754F47D81 CRC64;
MSSMASVLFA ALAISGVQVT PSRGYGCFPQ YSQFWGQYSP YFSLEGRSAI SSAVPPGCKI
TFAQSLQRHG ARFPTADKSA TYSSLIKRIQ EDATEFKDEF AFLKDYKYNL GADDLTPFGE
SQLYDSGINF FQRYHGLTKD SKVFVRSAGS ERVVASAHKF VEGFNKAKGS EKGGATKLDL
IISEEDRRKN PIAPQGCDAF DNDETADKIT DQFRSTFTQP IVDRVNKKLP GANIKIGDIK
SLMAMCPFDT VARTPDASKL SPFCHLFSHE EFRHYDYLET LGKFYGHGPG NSFGPAPGIG
YVNELIARLT SSPVKDNTTV DHELDDNPKT FPLGLPLYAD FSHDNSMTVI FTAMGLFNAT
KPLSPTKITD PADASGYSAS WTVPFGARAY FEKMVCDHSP SAKQEYVRVL LNDRVFPLQD
CHTDFLGRCK LDDFINGLTY ARSNGNWDQC EVSPPK
//
