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Reviewed, UniProtKB/Swiss-Prot P34754 (PHYB_ASPNG)

Last modified January 20, 2009. Version 51. 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

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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 niger
Taxonomic identifier5061 [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.

Sequence similarities

Belongs to the histidine acid phosphatase family.

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Ontologies

Keywords
   DomainSignal
   Molecular functionHydrolase
   PTMGlycoprotein
   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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Ref.1
Chain20 – 4794603-phytase B
PRO_0000023974

Sites

Active site821Nucleophile By similarity
Active site3381Proton donor By similarity

Amino acid modifications

Glycosylation1061N-linked (GlcNAc...) Potential
Glycosylation1911N-linked (GlcNAc...) Potential
Glycosylation2271N-linked (GlcNAc...) Potential
Glycosylation2501N-linked (GlcNAc...) Potential
Glycosylation3151N-linked (GlcNAc...) Potential
Glycosylation4251N-linked (GlcNAc...) Potential
Glycosylation4421N-linked (GlcNAc...) Potential
Glycosylation4581N-linked (GlcNAc...) Potential

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Sequences

Sequence LengthMass (Da)Tools
P34754-1 [UniParc].

Last modified February 1, 1994. Version 1.
Checksum: 395D4DA2B50FDFC4

FASTA47952,612
        10         20         30         40         50         60 
MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG GNGPYSERVS 

        70         80         90        100        110        120 
YGIARDPPTG CEVDQVIMVK RHGERYPSPS AGKSIEEALA 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 LTASDVYNLI VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG 

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

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

       430        440        450        460        470 
CPLANYTSIL NKNLPDYTTT CNVSASYPQY LSFWWNYNTT TELNYRSSPI ACQEGDAMD

« Hide

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References

[1]"Identification and cloning of a second phytase gene (phyB) from Aspergillus niger (ficuum)."
Ehrlich K.C., Montalbano B.G., Mullaney E.J., Dischinger H.C. Jr., Ullah A.H.J.
Biochem. Biophys. Res. Commun. 195:53-57(1993) [PubMed: 7916610] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 20-101; 133-141 AND 376-399.

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Cross-references

Sequence databases

L20567 Unassigned DNA. Translation: AAA02934.1.

3D structure databases

HSSPHSSP built from PDB template 1QFX based on UniProtKB P34755.
SMRP34754. Positions 33-479.
ModBaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.8. 277.

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_ASPNG
AccessionPrimary (citable) accession number: P34754
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: February 1, 1994
Last modified: January 20, 2009
This is version 51 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

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