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P81440 (PHYB_ASPFI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 52. 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 B

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

Protein attributes

Sequence length28 AA.
Sequence statusFragment.
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: 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

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 [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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRJN0715.

3D structure databases

ProteinModelPortalP81440.
SMRP81440. Positions 1-28.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000560. His_Pase_superF_clade-2.
[Graphical view]
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[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: April 16, 2014
This is version 52 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