ID   PHYB_ASPFI              Reviewed;          28 AA.
AC   P81440;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   15-DEC-1998, sequence version 1.
DT   22-FEB-2023, entry version 69.
DE   RecName: Full=3-phytase B;
DE            EC=3.1.3.8;
DE   AltName: Full=3 phytase B;
DE   AltName: Full=Myo-inositol hexakisphosphate phosphohydrolase B;
DE   AltName: Full=Myo-inositol-hexaphosphate 3-phosphohydrolase B;
DE   Flags: Fragment;
GN   Name=phyB;
OS   Aspergillus ficuum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX   NCBI_TaxID=5058;
RN   [1]
RP   PROTEIN SEQUENCE.
RX   PubMed=8484781; DOI=10.1006/bbrc.1993.1478;
RA   Ullah A.H., Dischinger H.C. Jr.;
RT   "Identification of active-site residues in Aspergillus ficuum extracellular
RT   pH 2.5 optimum acid phosphatase.";
RL   Biochem. Biophys. Res. Commun. 192:754-759(1993).
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   -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC       {ECO:0000305}.
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DR   PIR; JN0715; JN0715.
DR   AlphaFoldDB; P81440; -.
DR   SMR; P81440; -.
DR   GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.50.1240; Phosphoglycerate mutase-like; 1.
DR   InterPro; IPR033379; Acid_Pase_AS.
DR   InterPro; IPR029033; His_PPase_superfam.
DR   SUPFAM; SSF53254; Phosphoglycerate mutase-like; 1.
DR   PROSITE; PS00616; HIS_ACID_PHOSPHAT_1; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase.
FT   CHAIN           <1..>28
FT                   /note="3-phytase B"
FT                   /id="PRO_0000114471"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        17
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         28
SQ   SEQUENCE   28 AA;  3114 MW;  675340A707C57CD8 CRC64;
     RDPTGCEVDQ VIMVKRHGER YPSPSAGK
//