PHYB_ASPFI
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 25-MAY-2022, entry version 67.
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; -; 1.
DR InterPro; IPR033379; Acid_Pase_AS.
DR InterPro; IPR029033; His_PPase_superfam.
DR SUPFAM; SSF53254; SSF53254; 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