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O31097 (PHYC_BACIU) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 69. 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

EC=3.1.3.8
Alternative name(s):
MYO-inositol-hexaphosphate 3-phosphohydrolase
Phytate 3-phosphatase
Gene names
Name:phyC
Synonyms:phyB13
OrganismBacillus subtilis
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length383 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. Only phytate, ADP, and ATP were hydrolyzed (100, 75, and 50% of the relative activity, respectively).

Catalytic activity

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

Cofactor

Calcium. Required for its activity and/or stability.

Subcellular location

Secreted.

Induction

By phytate.

Sequence similarities

Contains 1 BPP (beta-propeller phytase) domain.

Biophysicochemical properties

pH dependence:

Optimum pH is 7.

Temperature dependence:

Optimum temperature is 55 degrees Celsius.

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: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Potential
Propeptide27 – 293
PRO_0000022055
Chain30 – 3833543-phytase
PRO_0000022056

Regions

Domain30 – 362333BPP

Secondary structure

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

Details...

Sequences

Sequence LengthMass (Da)Tools
O31097 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: E9BEC2E4A48EB9CA

FASTA38341,923
        10         20         30         40         50         60 
MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA GDAADDPAIW 

        70         80         90        100        110        120 
LDPKTPQNSK LITTNKKSGL VVYSLDGKML HSYNTGKLNN VDIRYDFPLN GKKVDIAAAS 

       130        140        150        160        170        180 
NRSEGKNTIE IYAIDGKNGT LQSMTDPDHP IATAINEVYG FTLYHSQKTG KYYAMVTGKE 

       190        200        210        220        230        240 
GEFEQYELKA DKNGYISGKK VRAFKMNSQT EGMAADDEYG RLYIAEEDEA IWKFSAEPDG 

       250        260        270        280        290        300 
GSNGTVIDRA DGRHLTRDIE GLTIYYAADG KGYLMASSQG NSSYAIYDRQ GKNKYVADFR 

       310        320        330        340        350        360 
ITDGPETDGT SDTDGIDVLG FGLGPEYPFG IFVAQDGENI DHGQKANQNF KIVPWERIAD 

       370        380 
QIGFRPLANE QVDPRKLTDR SGK 

« Hide

References

[1]"Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis."
Kerovuo J., Lauraeus M., Nurminen P., Kalkkinen N., Apajalahti J.
Appl. Environ. Microbiol. 64:2079-2085(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
Strain: VTT-E-68013.
[2]"Cloning of neutral phytase gene nphy from Bacillus subtilis and its expression in Escherichia coli."
Yao B., Yuan T., Wang Y., Fan Y.
Chin. J. Biotechnol. 17:11-15(2001)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 981.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF029053 Genomic DNA. Translation: AAC31775.1.
AJ277890 Genomic DNA. Translation: CAB91845.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3AMRX-ray1.25A29-383[»]
3AMSX-ray2.08A29-383[»]
ProteinModelPortalO31097.
SMRO31097. Positions 29-381.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D2.120.10.20. 1 hit.
InterProIPR003431. b_Phytase.
[Graphical view]
PfamPF02333. Phytase. 1 hit.
[Graphical view]
PROSITEPS51662. BP_PHYTASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO31097.

Entry information

Entry namePHYC_BACIU
AccessionPrimary (citable) accession number: O31097
Entry history
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references