ID   PHYA_THETO              Reviewed;         487 AA.
AC   O00107;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-1997, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=3-phytase A;
DE            EC=3.1.3.8;
DE   AltName: Full=3 phytase A;
DE   AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase A;
DE   AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase A;
DE   Flags: Precursor;
GN   Name=PHYA;
OS   Thermothelomyces thermophilus (Myceliophthora thermophila).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Chaetomiaceae; Thermothelomyces.
OX   NCBI_TaxID=78579;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION.
RX   PubMed=9025298; DOI=10.1099/00221287-143-1-245;
RA   Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., van Loon A.P.G.M.;
RT   "The phytase subfamily of histidine acid phosphatases: isolation of genes
RT   for two novel phytases from the fungi Aspergillus terreus and
RT   Myceliophthora thermophila.";
RL   Microbiology 143:245-252(1997).
CC   -!- FUNCTION: Catalyzes the hydrolysis of inorganic orthophosphate from
CC       phytate.
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.5-6.0. Active from 3.5 to 8.5 with phytic acid as
CC         substrate. The optimum pH is shifted to more acidic values with 4-
CC         nitrophenyl phosphate as substrate.;
CC   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   EMBL; U59806; AAB52508.1; -; Genomic_DNA.
DR   AlphaFoldDB; O00107; -.
DR   SMR; O00107; -.
DR   VEuPathDB; FungiDB:MYCTH_104551; -.
DR   BRENDA; 3.1.3.8; 13804.
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   Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..487
FT                   /note="3-phytase A"
FT                   /id="PRO_0000023973"
FT   ACT_SITE        75
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        369
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        165
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        247
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        346
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..35
FT                   /evidence="ECO:0000250"
FT   DISULFID        64..421
FT                   /evidence="ECO:0000250"
FT   DISULFID        208..485
FT                   /evidence="ECO:0000250"
FT   DISULFID        260..289
FT                   /evidence="ECO:0000250"
FT   DISULFID        456..464
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   487 AA;  52538 MW;  97D10EDC83D051DB CRC64;
     MTGLGVMVVM VGFLAIASLQ SESRPCDTPD LGFQCGTAIS HFWGQYSPYF SVPSELDASI
     PDDCEVTFAQ VLSRHGARAP TLKRAASYVD LIDRIHHGAI SYGPGYEFLR TYDYTLGADE
     LTRTGQQQMV NSGIKFYRRY RALARKSIPF VRTAGQDRVV HSAENFTQGF HSALLADRGS
     TVRPTLPYDM VVIPETAGAN NTLHNDLCTA FEEGPYSTIG DDAQDTYLST FAGPITARVN
     ANLPGANLTD ADTVALMDLC PFETVASSSS DPATADAGGG NGRPLSPFCR LFSESEWRAY
     DYLQSVGKWY GYGPGNPLGP TQGVGFVNEL LARLAGVPVR DGTSTNRTLD GDPRTFPLGR
     PLYADFSHDN DMMGVLGALG AYDGVPPLDK TARRDPEELG GYAASWAVPF AARIYVEKMR
     CSGGGGGGGG GEGRQEKDEE MVRVLVNDRV MTLKGCGADE RGMCTLERFI ESMAFARGNG
     KWDLCFA