ID   PHYB_ASPNG              Reviewed;         479 AA.
AC   P34754;
DT   01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1994, sequence version 1.
DT   25-MAY-2022, entry version 91.
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: Precursor;
GN   Name=phyB;
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 20-101; 133-141
RP   AND 376-399.
RX   PubMed=7916610; DOI=10.1006/bbrc.1993.2008;
RA   Ehrlich K.C., Montalbano B.G., Mullaney E.J., Dischinger H.C. Jr.,
RA   Ullah A.H.J.;
RT   "Identification and cloning of a second phytase gene (phyB) from
RT   Aspergillus niger (ficuum).";
RL   Biochem. Biophys. Res. Commun. 195:53-57(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}.
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; L20567; AAA02934.1; -; Unassigned_DNA.
DR   AlphaFoldDB; P34754; -.
DR   SMR; P34754; -.
DR   STRING; 5061.CADANGAP00007284; -.
DR   Allergome; 3131; Asp n 25.0101.
DR   Allergome; 844; Asp n 25.
DR   VEuPathDB; FungiDB:An08g11030; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1189246; -.
DR   VEuPathDB; FungiDB:ATCC64974_96640; -.
DR   VEuPathDB; FungiDB:M747DRAFT_325681; -.
DR   eggNOG; KOG1382; Eukaryota.
DR   BRENDA; 3.1.3.8; 518.
DR   GO; GO:0016158; F:3-phytase activity; IEA:UniProtKB-EC.
DR   CDD; cd07061; HP_HAP_like; 1.
DR   Gene3D; 3.40.50.1240; -; 3.
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   Direct protein sequencing; Glycoprotein; Hydrolase; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000269|PubMed:7916610"
FT   CHAIN           20..479
FT                   /note="3-phytase B"
FT                   /id="PRO_0000023974"
FT   ACT_SITE        82
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        338
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        106
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        191
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        227
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        250
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        315
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        425
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        442
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        458
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   479 AA;  52612 MW;  395D4DA2B50FDFC4 CRC64;
     MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG GNGPYSERVS
     YGIARDPPTG CEVDQVIMVK RHGERYPSPS AGKSIEEALA KVYSINTTEY KGDLAFLNDW
     TYYVPNECYY NAETTSGPYA GLLDAYNHGN DYKARYGHLW NGETVVPFFS SGYGRVIETA
     RKFGEGFFGY NYSTNAALNI ISESEVMGAD SLTPTCDTDN DQTTCDNLTY QLPQFKVAAA
     RLNSQNPGMN LTASDVYNLI VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG
     PGDKNMAAVG AVYANASLTL LNQGPKEAGP LFFNFAHDTN ITPILAALGV LIPNEDLPLD
     RVAFGNPYSI GNIVPMGGHL TIERLSCQAT ALSDKGTYVR LVLNEAVLPF NDCTSGPGYS
     CPLANYTSIL NKNLPDYTTT CNVSASYPQY LSFWWNYNTT TELNYRSSPI ACQEGDAMD