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P34753 (PHYA_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 70. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:phyA
Synonyms:phy
OrganismAspergillus awamori (Black koji mold)
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length467 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

Catalytic activity

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

Subcellular location

Secreted.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-phytase activity

Inferred from electronic annotation. Source: UniProtKB-EC

acid phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 4674443-phytase A
PRO_0000023971

Sites

Active site821Nucleophile By similarity
Active site3621Proton donor By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation591N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Glycosylation3881N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 40 By similarity
Disulfide bond71 ↔ 414 By similarity
Disulfide bond215 ↔ 465 By similarity
Disulfide bond264 ↔ 282 By similarity
Disulfide bond436 ↔ 444 By similarity

Sequences

Sequence LengthMass (Da)Tools
P34753 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 118E828A5D7EC661

FASTA46751,075
        10         20         30         40         50         60 
MGVSAVLLPL YLLAGVTSGL AVPASRNQST CDTVDQGYQC FSETSHLWGQ YAPFFSLANE 

        70         80         90        100        110        120 
SAISPDVPAG CRVTFAQVLS RHGARYPTES KGKKYSALIE EIQQNVTTFD GKYAFLKTYN 

       130        140        150        160        170        180 
YSLGADDLTP FGEQELVNSG IKFYQRYESL TRNIIPFIRS SGSSRVIASG EKFIEGFQST 

       190        200        210        220        230        240 
KLKDPRAQPG QSSPKIDVVI SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFAPSIR 

       250        260        270        280        290        300 
QRLENDLSGV TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW IHYDYLQSLK 

       310        320        330        340        350        360 
KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSNPATFP LNSTLYADFS 

       370        380        390        400        410        420 
HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT VPFASRLYVE MMQCQAEQEP 

       430        440        450        460 
LVRVLVNDRV VPLHGCPIDA LGRCTRDSFV RGLSFARSGG DWAECSA 

« Hide

References

[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(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ALK0243.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02421 Unassigned DNA. Translation: AAA16898.1.
PIRJN0889.

3D structure databases

ProteinModelPortalP34753.
SMRP34753. Positions 30-467.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHYA_ASPAW
AccessionPrimary (citable) accession number: P34753
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 70 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families