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Reviewed, UniProtKB/Swiss-Prot P34755 (PHYB_ASPAW)

Last modified March 3, 2009. Version 58. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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

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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
Taxonomic identifier105351 [NCBI]
Taxonomic lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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Protein attributes

Sequence length479 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

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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.

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Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
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...

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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

1 ................................................................. 479
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
P34755-1 [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

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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: 8224894] [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: 10329192] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

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Cross-references

Sequence databases

L02420 Unassigned DNA. Translation: AAA16897.1.
PIRJN0890.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QFXX-ray2.40A/B20-479[»]
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.8. 15245.

Family and domain databases

InterProIPR000560. Histidine_acid_Pase.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. Acid_phosphat_A. 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...

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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: March 3, 2009
This is version 58 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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