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Protein

3-phytase B

Gene

phyB

Organism
Aspergillus ficuum
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

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 sitei17 – 171NucleophileBy similarity

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:phyB
OrganismiAspergillus ficuum
Taxonomic identifieri5058 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini‹1 – ›28›283-phytase BPRO_0000114471Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliP81440.
SMRiP81440. Positions 1-28.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Family and domain databases

InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Fragment.

P81440-1 [UniParc]FASTAAdd to basket

« Hide

        10         20 
RDPTGCEVDQ VIMVKRHGER YPSPSAGK
Length:28
Mass (Da):3,114
Last modified:December 15, 1998 - v1
Checksum:i675340A707C57CD8
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei1 – 11
Non-terminal residuei28 – 281

Sequence databases

PIRiJN0715.

Cross-referencesi

Sequence databases

PIRiJN0715.

3D structure databases

ProteinModelPortaliP81440.
SMRiP81440. Positions 1-28.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
[Graphical view]
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiPHYB_ASPFI
AccessioniPrimary (citable) accession number: P81440
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: December 15, 1998
Last modified: October 1, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

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.