PHYA_ASPAW
ID PHYA_ASPAW Reviewed; 467 AA.
AC P34753;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1994, 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; Synonyms=phy;
OS Aspergillus awamori (Black koji mold).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=105351;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ALK0243;
RX PubMed=8224894; DOI=10.1016/0378-1119(93)90224-q;
RA Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A.,
RA Miettinen-Oinonen A., Nevalainen H., Rambosek J.A.;
RT "The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-
RT optimum acid phosphatase (aph) from Aspergillus niger var. awamori.";
RL Gene 133:55-62(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 -!- SUBCELLULAR LOCATION: Secreted.
CC -!- SIMILARITY: Belongs to the histidine acid phosphatase family.
CC {ECO:0000305}.
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DR EMBL; L02421; AAA16898.1; -; Unassigned_DNA.
DR PIR; JN0889; JN0889.
DR AlphaFoldDB; P34753; -.
DR SMR; P34753; -.
DR BRENDA; 3.1.3.26; 494.
DR BRENDA; 3.1.3.8; 494.
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 3: Inferred from homology;
KW Disulfide bond; Glycoprotein; Hydrolase; Secreted; Signal.
FT SIGNAL 1..23
FT /evidence="ECO:0000255"
FT CHAIN 24..467
FT /note="3-phytase A"
FT /id="PRO_0000023971"
FT ACT_SITE 82
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 362
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 27
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 59
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 105
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 120
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 207
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 230
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 339
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 352
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 376
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 388
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 31..40
FT /evidence="ECO:0000250"
FT DISULFID 71..414
FT /evidence="ECO:0000250"
FT DISULFID 215..465
FT /evidence="ECO:0000250"
FT DISULFID 264..282
FT /evidence="ECO:0000250"
FT DISULFID 436..444
FT /evidence="ECO:0000250"
SQ SEQUENCE 467 AA; 51075 MW; 118E828A5D7EC661 CRC64;
MGVSAVLLPL YLLAGVTSGL AVPASRNQST CDTVDQGYQC FSETSHLWGQ YAPFFSLANE
SAISPDVPAG CRVTFAQVLS RHGARYPTES KGKKYSALIE EIQQNVTTFD GKYAFLKTYN
YSLGADDLTP FGEQELVNSG IKFYQRYESL TRNIIPFIRS SGSSRVIASG EKFIEGFQST
KLKDPRAQPG QSSPKIDVVI SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFAPSIR
QRLENDLSGV TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW IHYDYLQSLK
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSNPATFP LNSTLYADFS
HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT VPFASRLYVE MMQCQAEQEP
LVRVLVNDRV VPLHGCPIDA LGRCTRDSFV RGLSFARSGG DWAECSA
