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Protein

3-phytase A

Gene

phyA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

Catalytic activityi

Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei82 – 821NucleophileBy similarity
Active sitei362 – 3621Proton donorBy similarity

GO - Molecular functioni

  1. 3-phytase activity Source: UniProtKB-EC
  2. acid phosphatase activity Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.26. 494.
3.1.3.8. 494.

Names & Taxonomyi

Protein namesi
Recommended name:
3-phytase A (EC:3.1.3.8)
Alternative name(s):
3 phytase A
Myo-inositol hexakisphosphate phosphohydrolase A
Myo-inositol-hexaphosphate 3-phosphohydrolase A
Gene namesi
Name:phyA
Synonyms:phy
OrganismiAspergillus awamori (Black koji mold)
Taxonomic identifieri105351 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2323Sequence AnalysisAdd
BLAST
Chaini24 – 4674443-phytase APRO_0000023971Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Glycosylationi27 – 271N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi31 ↔ 40By similarity
Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi71 ↔ 414By similarity
Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi215 ↔ 465By similarity
Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi264 ↔ 282By similarity
Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi436 ↔ 444By similarity

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

3D structure databases

ProteinModelPortaliP34753.
SMRiP34753. Positions 30-467.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P34753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGVSAVLLPL YLLAGVTSGL AVPASRNQST CDTVDQGYQC FSETSHLWGQ
60 70 80 90 100
YAPFFSLANE SAISPDVPAG CRVTFAQVLS RHGARYPTES KGKKYSALIE
110 120 130 140 150
EIQQNVTTFD GKYAFLKTYN YSLGADDLTP FGEQELVNSG IKFYQRYESL
160 170 180 190 200
TRNIIPFIRS SGSSRVIASG EKFIEGFQST KLKDPRAQPG QSSPKIDVVI
210 220 230 240 250
SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFAPSIR QRLENDLSGV
260 270 280 290 300
TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW IHYDYLQSLK
310 320 330 340 350
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSNPATFP
360 370 380 390 400
LNSTLYADFS HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT
410 420 430 440 450
VPFASRLYVE MMQCQAEQEP LVRVLVNDRV VPLHGCPIDA LGRCTRDSFV
460
RGLSFARSGG DWAECSA
Length:467
Mass (Da):51,075
Last modified:February 1, 1994 - v1
Checksum:i118E828A5D7EC661
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02421 Unassigned DNA. Translation: AAA16898.1.
PIRiJN0889.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L02421 Unassigned DNA. Translation: AAA16898.1.
PIRiJN0889.

3D structure databases

ProteinModelPortaliP34753.
SMRiP34753. Positions 30-467.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.3.26. 494.
3.1.3.8. 494.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori."
    Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A., Miettinen-Oinonen A., Nevalainen H., Rambosek J.A.
    Gene 133:55-62(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: ALK0243.

Entry informationi

Entry nameiPHYA_ASPAW
AccessioniPrimary (citable) accession number: P34753
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 1, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.