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   25-MAY-2022, entry version 42.
DE   RecName: Full=3-phytase A {ECO:0000250|UniProtKB:P34752};
DE            EC=3.1.3.8 {ECO:0000250|UniProtKB:P34752};
DE   AltName: Full=Allergen Asp n 25 homolog {ECO:0000305};
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 hydrolysis of inorganic orthophosphate from
CC       phytate. {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   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:21919205}.
CC   -!- ALLERGEN: May cause an allergic reaction in human. {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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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   PRIDE; D4ANW6; -.
DR   EnsemblFungi; EFE34977; EFE34977; ARB_05933.
DR   GeneID; 9525903; -.
DR   KEGG; abe:ARB_05933; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   HOGENOM; CLU_020880_0_0_1; -.
DR   OMA; YLMDLCP; -.
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; -; 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   Pfam; PF00328; His_Phos_2; 1.
DR   PIRSF; PIRSF000894; Acid_phosphatase; 1.
DR   SUPFAM; SSF53254; SSF53254; 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="3-phytase A"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434430"
FT   ACT_SITE        69
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000894-1"
FT   ACT_SITE        344
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PIRSR:PIRSR000894-1"
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:P34752"
FT   DISULFID        197..450
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   DISULFID        246..264
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
FT   DISULFID        421..429
FT                   /evidence="ECO:0000250|UniProtKB:P34752"
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