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Reviewed, UniProtKB/Swiss-Prot P81440 (PHYB_ASPFI)

Last modified January 20, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    3-phytase B
    EC=3.1.3.8
Alternative name(s):
    3 phytase B
    Myo-inositol-hexaphosphate 3-phosphohydrolase B
    Myo-inositol hexakisphosphate phosphohydrolase B
Gene names
Name: phyB
OrganismAspergillus ficuum
Taxonomic identifier5058 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesTrichocomaceaemitosporic TrichocomaceaeAspergillus

Protein attributes

Sequence length28 AA.
Sequence statusFragment.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

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.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   Molecular functionHydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Molecular function3-phytase activity

Inferred from electronic annotation. Source: EC

acid phosphatase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain‹1 – ›28›283-phytase B
PRO_0000114471

Sites

Active site171Nucleophile By similarity

Experimental info

Non-terminal residue11
Non-terminal residue281

Sequences

Sequence LengthMass (Da)Tools
P81440-1 [UniParc].

Last modified December 15, 1998. Version 1.
Checksum: 675340A707C57CD8

FASTA283,114
        10         20 
RDPTGCEVDQ VIMVKRHGER YPSPSAGK 

« Hide

References

[1]"Identification of active-site residues in Aspergillus ficuum extracellular pH 2.5 optimum acid phosphatase."
Ullah A.H., Dischinger H.C. Jr.
Biochem. Biophys. Res. Commun. 192:754-759(1993) [PubMed: 8484781] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRJN0715.

3D structure databases

HSSPHSSP built from PDB template 1QFX based on UniProtKB P34755.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.8. 81696.

Family and domain databases

InterProIPR000560. Histidine_acid_Pase.
[Graphical view]
PfamPF00328. Acid_phosphat_A. 1 hit.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. Partial match.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePHYB_ASPFI
AccessionPrimary (citable) accession number: P81440
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: January 20, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents