PHYA_ASPOR
ID PHYA_ASPOR Reviewed; 466 AA.
AC Q9C1T1; Q2UGV7;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 25-MAY-2022, entry version 88.
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; ORFNames=AO090023000692;
OS Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=510516;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Gomi K.;
RT "Nucleotide sequence of Aspergillus oryzae phytase cDNA.";
RL Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 42149 / RIB 40;
RX PubMed=16372010; DOI=10.1038/nature04300;
RA Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA Takahashi M., Takase K., Terabayashi Y., Wortman J.R., Yamada O.,
RA Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA Kikuchi H.;
RT "Genome sequencing and analysis of Aspergillus oryzae.";
RL Nature 438:1157-1161(2005).
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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; AB042805; BAB40715.1; -; mRNA.
DR EMBL; AP007157; BAE59208.1; -; Genomic_DNA.
DR RefSeq; XP_001821210.1; XM_001821158.2.
DR AlphaFoldDB; Q9C1T1; -.
DR SMR; Q9C1T1; -.
DR EnsemblFungi; BAE59208; BAE59208; AO090023000692.
DR GeneID; 5993212; -.
DR KEGG; aor:AO090023000692; -.
DR HOGENOM; CLU_020880_0_0_1; -.
DR Proteomes; UP000006564; Chromosome 3.
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 2: Evidence at transcript level;
KW Disulfide bond; Glycoprotein; Hydrolase; Reference proteome; Secreted;
KW Signal.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..466
FT /note="3-phytase A"
FT /id="PRO_0000043346"
FT ACT_SITE 81
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 361
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 104
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 119
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 206
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 219
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 338
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 351
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 375
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 30..39
FT /evidence="ECO:0000250"
FT DISULFID 70..413
FT /evidence="ECO:0000250"
FT DISULFID 214..464
FT /evidence="ECO:0000250"
FT DISULFID 263..281
FT /evidence="ECO:0000250"
FT DISULFID 435..443
FT /evidence="ECO:0000250"
SQ SEQUENCE 466 AA; 51257 MW; 8033BED57FBA2791 CRC64;
MAVLSVLLPI TFLLSSVTGT PVTSPRQQSC NTVDEGYQCF SGVSHLWGQY SPYFSVDDES
SLSEDVPDHC QVTFAQVLSR HGARYPTKSK SEKYAKLIKA VQHNATSFSG KYAFLKSYNY
SLGADDLTPF GENQLVDSGI KFYQRYEELA KNVVPFIRAS GSDRVIASGE KFIEGFQKAK
LGDSKSKRGQ PAPIVNVVIT ETEGFNNTLD HSLCTAFENS TTGDDAEDKF TAVFTPSIVE
RLEKDLPGTT LSSKEVVYLM DMCSFDTIAL TRDGSRLSPF CALFTQEEWA QYDYLQSVSK
YYGYGGGNPL GPAQGIGFAN ELIARLTKSP VKDHTTTNTT LDSNPATFPL NATLYADFSH
DNTMTSVFFA LGLYNTTEPL SQTSVQSTEE TNGYSSARTV PFGARAYVEM MQCTDEKEPL
VRVLVNDRVI PLQGCDADEY GRCKRDDFVE GLSFVTSGGN WGECFA
