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P34755 (PHYB_ASPAW) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 72. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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):
Myo-inositol-hexaphosphate 3-phosphohydrolase B
pH 2.5 optimum acid phosphatase
Gene names
Name:phyB
Synonyms:aph
OrganismAspergillus awamori (Black koji mold)
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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.

Subunit structure

Homodimer.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
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

Signal peptide1 – 1919 By similarity
Chain20 – 4794603-phytase B
PRO_0000023975

Sites

Active site821Nucleophile
Active site3381Proton donor

Amino acid modifications

Glycosylation1911N-linked (GlcNAc...)
Glycosylation3151N-linked (GlcNAc...)
Glycosylation4581N-linked (GlcNAc...)
Disulfide bond71 ↔ 387
Disulfide bond128 ↔ 472
Disulfide bond216 ↔ 441
Disulfide bond225 ↔ 298
Disulfide bond413 ↔ 421

Secondary structure

................................................................. 479
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P34755 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 4F8E0F3778CC3B08

FASTA47952,678
        10         20         30         40         50         60 
MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG GNGPYSERVS 

        70         80         90        100        110        120 
YGIARDPPTS CEVDQVIMVK RHGERYPSPS AGKDIEEALA KVYSINTTEY KGDLAFLNDW 

       130        140        150        160        170        180 
TYYVPNECYY NAETTSGPYA GLLDAYNHGN DYKARYGHLW NGETVVPFFS SGYGRVIETA 

       190        200        210        220        230        240 
RKFGEGFFGY NYSTNAALNI ISESEVMGAD SLTPTCDTDN DQTTCDNLTY QLPQFKVAAA 

       250        260        270        280        290        300 
RLNSQNPGMN LTASDVYNLM VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG 

       310        320        330        340        350        360 
PGDKNMAAVG AVYANASLTL LNQGPKEAGS LFFNFAHDTN ITPILAALGV LIPNEDLPLD 

       370        380        390        400        410        420 
RVAFGNPYSI GNIVPMGGHL TIERLSCQAT ALSDEGTYVR LVLNEAVLPF NDCTSGPGYS 

       430        440        450        460        470 
CPLANYTSIL NKNLPDYTTT CNVSASYPQY LSFWWNYNTT TELNYRSSPI ACQEGDAMD 

« 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.
[2]"Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4-A resolution."
Kostrewa D., Wyss M., D'Arcy A., van Loon A.P.G.M.
J. Mol. Biol. 288:965-974(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L02420 Unassigned DNA. Translation: AAA16897.1.
PIRJN0890.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QFXX-ray2.40A/B20-479[»]
ProteinModelPortalP34755.
SMRP34755. Positions 33-479.
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...

Other

EvolutionaryTraceP34755.

Entry information

Entry namePHYB_ASPAW
AccessionPrimary (citable) accession number: P34755
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: April 16, 2014
This is version 72 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references