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O00107 (PHYA_THIHE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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 A

EC=3.1.3.8
Alternative name(s):
3 phytase A
Myo-inositol hexakisphosphate phosphohydrolase A
Myo-inositol-hexaphosphate 3-phosphohydrolase A
Gene names
Name:PHYA
OrganismThielavia heterothallica (Myceliophthora thermophila)
Taxonomic identifier78579 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora

Protein attributes

Sequence length487 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.

Subcellular location

Secreted.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.5-6.0. Active from 3.5 to 8.5 with phytic acid as substrate. The optimum pH is shifted to more acidic values with 4-nitrophenyl phosphate as substrate.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   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 Potential
Chain20 – 4874683-phytase A
PRO_0000023973

Regions

Compositional bias423 – 43311Poly-Gly

Sites

Active site751Nucleophile By similarity
Active site3691Proton donor By similarity

Amino acid modifications

Glycosylation1651N-linked (GlcNAc...) Potential
Glycosylation2001N-linked (GlcNAc...) Potential
Glycosylation2471N-linked (GlcNAc...) Potential
Glycosylation3461N-linked (GlcNAc...) Potential
Disulfide bond26 ↔ 35 By similarity
Disulfide bond64 ↔ 421 By similarity
Disulfide bond208 ↔ 485 By similarity
Disulfide bond260 ↔ 289 By similarity
Disulfide bond456 ↔ 464 By similarity

Sequences

Sequence LengthMass (Da)Tools
O00107 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 97D10EDC83D051DB

FASTA48752,538
        10         20         30         40         50         60 
MTGLGVMVVM VGFLAIASLQ SESRPCDTPD LGFQCGTAIS HFWGQYSPYF SVPSELDASI 

        70         80         90        100        110        120 
PDDCEVTFAQ VLSRHGARAP TLKRAASYVD LIDRIHHGAI SYGPGYEFLR TYDYTLGADE 

       130        140        150        160        170        180 
LTRTGQQQMV NSGIKFYRRY RALARKSIPF VRTAGQDRVV HSAENFTQGF HSALLADRGS 

       190        200        210        220        230        240 
TVRPTLPYDM VVIPETAGAN NTLHNDLCTA FEEGPYSTIG DDAQDTYLST FAGPITARVN 

       250        260        270        280        290        300 
ANLPGANLTD ADTVALMDLC PFETVASSSS DPATADAGGG NGRPLSPFCR LFSESEWRAY 

       310        320        330        340        350        360 
DYLQSVGKWY GYGPGNPLGP TQGVGFVNEL LARLAGVPVR DGTSTNRTLD GDPRTFPLGR 

       370        380        390        400        410        420 
PLYADFSHDN DMMGVLGALG AYDGVPPLDK TARRDPEELG GYAASWAVPF AARIYVEKMR 

       430        440        450        460        470        480 
CSGGGGGGGG GEGRQEKDEE MVRVLVNDRV MTLKGCGADE RGMCTLERFI ESMAFARGNG 


KWDLCFA 

« Hide

References

[1]"The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila."
Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., van Loon A.P.G.M.
Microbiology 143:245-252(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59806 Genomic DNA. Translation: AAB52508.1.

3D structure databases

ProteinModelPortalO00107.
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...

Entry information

Entry namePHYA_THIHE
AccessionPrimary (citable) accession number: O00107
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 62 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