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Reviewed, UniProtKB/Swiss-Prot O66037 (PHYT_BACSD)

Last modified June 16, 2009. Version 52. 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
    EC=3.1.3.8
Alternative name(s):
    Phytate 3-phosphatase
    Myo-inositol-hexaphosphate 3-phosphohydrolase
Gene names
Name: phy
OrganismBacillus sp. (strain DS11)
Taxonomic identifier86035 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

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Protein attributes

Sequence length383 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)

Catalytic activity

Myo-inositol hexakisphosphate + H2O = 1D-myo-inositol 1,2,4,5,6-pentakisphosphate + phosphate.

Subcellular location

Secreted.

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Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular function3-phytase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 304 Ref.1
PRO_0000022058
Chain31 – 3833533-phytase
PRO_0000022059

Secondary structure

1 ....................................................................... 383
Helix Strand Turn

Details...

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Sequences

Sequence LengthMass (Da)Tools
O66037-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: DCB65188F7B61C8C

FASTA38341,802
        10         20         30         40         50         60 
MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA GDAADDPAIW 

        70         80         90        100        110        120 
LDPKNPQNSK LITTNKKSGL AVYSLEGKML HSYHTGKLNN VDIRYDFPLN GKKVDIAAAS 

       130        140        150        160        170        180 
NRSEGKNTIE IYAIDGKNGT LQSITDPNRP IASAIDEVYG FSLYHSQKTG KYYAMVTGKE 

       190        200        210        220        230        240 
GEFEQYELNA DKNGYISGKK VRAFKMNSQT EGMAADDEYG SLYIAEEDEA IWKFSAEPDG 

       250        260        270        280        290        300 
GSNGTVIDRA DGRHLTPDIE GLTIYYAADG KGYLLASSQG NSSYAIYERQ GQNKYVADFQ 

       310        320        330        340        350        360 
ITDGPETDGT SDTDGIDVLG FGLGPEYPFG LFVAQDGENI DHGQKANQNF KMVPWERIAD 

       370        380 
KIGFHPQVNK QVDPRKMTDR SGK

« Hide

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References

[1]"Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coli."
Kim Y.-O., Lee J.-K., Kim H.-K., Yu J.-H., Oh T.-K.
FEMS Microbiol. Lett. 162:185-191(1998) [PubMed: 9595681] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-44 AND 214-223.
[2]"Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain."
Ha N.-C., Kim Y.-O., Oh T.-K., Oh B.-H.
Acta Crystallogr. D 55:691-693(1999) [PubMed: 10089471] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
[3]"Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states."
Ha N.-C., Oh B.-C., Shin S., Kim H.-J., Oh T.-K., Kim Y.-O., Choi K.Y., Oh B.-H.
Nat. Struct. Biol. 7:147-153(2000) [PubMed: 10655618] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
+Additional computationally mapped references.

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Cross-references

Sequence databases

U85968 Genomic DNA. Translation: AAC38573.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1CVMX-ray2.40A29-381[»]
1H6LX-ray1.80A29-381[»]
1POOX-ray2.10A29-383[»]
1QLGX-ray2.20A29-383[»]
2POOX-ray2.05A29-383[»]
ModBaseSearch...

Family and domain databases

InterProIPR003431. Phytase.
[Graphical view]
PfamPF02333. Phytase. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry namePHYT_BACSD
AccessionPrimary (citable) accession number: O66037
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 1, 1998
Last modified: June 16, 2009
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents