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O00085 (PHYA1_ASPTE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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
OrganismAspergillus terreus
Taxonomic identifier33178 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length466 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. Releases 5 of the 6 phosphate groups to yield the end product myo-inositol 2-monophosphate. Specific for phytate. Ref.3

Catalytic activity

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

Subunit structure

Monomer. Ref.2

Subcellular location

Secreted.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=10.6 µM for phytate Ref.3

pH dependence:

Optimum pH is 5.5. Active from 2.5 to 7.5 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
   Technical termDirect 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

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 By similarity
Chain20 – 4664473-phytase A
PRO_0000023972

Sites

Active site821Nucleophile By similarity
Active site3621Proton donor By similarity

Amino acid modifications

Glycosylation1201N-linked (GlcNAc...) Potential
Glycosylation2071N-linked (GlcNAc...) Potential
Glycosylation2301N-linked (GlcNAc...) Potential
Glycosylation3391N-linked (GlcNAc...) Potential
Glycosylation3521N-linked (GlcNAc...) Potential
Glycosylation3761N-linked (GlcNAc...) Potential
Disulfide bond31 ↔ 40 By similarity
Disulfide bond71 ↔ 414 By similarity
Disulfide bond215 ↔ 465 By similarity
Disulfide bond264 ↔ 282 By similarity
Disulfide bond436 ↔ 444 By similarity

Sequences

Sequence LengthMass (Da)Tools
O00085 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 21CDCB559C96AE66

FASTA46651,093
        10         20         30         40         50         60 
MGFLAIVLSV ALLFRSTSGT PLGPRGKHSD CNSVDHGYQC FPELSHKWGL YAPYFSLQDE 

        70         80         90        100        110        120 
SPFPLDVPED CHITFVQVLA RHGARSPTHS KTKAYAATIA AIQKSATAFP GKYAFLQSYN 

       130        140        150        160        170        180 
YSLDSEELTP FGRNQLRDLG AQFYERYNAL TRHINPFVRA TDASRVHESA EKFVEGFQTA 

       190        200        210        220        230        240 
RQDDHHANPH QPSPRVDVAI PEGSAYNNTL EHSLCTAFES STVGDDAVAN FTAVFAPAIA 

       250        260        270        280        290        300 
QRLEADLPGV QLSTDDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTATEW TQYNYLLSLD 

       310        320        330        340        350        360 
KYYGYGGGNP LGPVQGVGWA NELMARLTRA PVHDHTCVNN TLDASPATFP LNATLYADFS 

       370        380        390        400        410        420 
HDSNLVSIFW ALGLYNGTAP LSQTSVESVS QTDGYAAAWT VPFAARAYVE MMQCRAEKEP 

       430        440        450        460 
LVRVLVNDRV MPLHGCPTDK LGRCKRDAFV AGLSFAQAGG NWADCF 

« 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.
Strain: 9A1.
[2]"Biophysical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): molecular size, glycosylation pattern, and engineering of proteolytic resistance."
Wyss M., Pasamontes L., Friedlein A., Remy R., Tessier M., Kronenberger A., Middendorf A., Lehmann M., Schnoebelen L., Roethlisberger U., Kusznir E., Wahl G., Mueller F., Lahm H.-W., Vogel K., van Loon A.P.G.M.
Appl. Environ. Microbiol. 65:359-366(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 29-38 AND 192-200, SUBUNIT.
Strain: 9A1.
[3]"Biochemical characterization of fungal phytases (myo-inositol hexakisphosphate phosphohydrolases): catalytic properties."
Wyss M., Brugger R., Kronenberger A., Remy R., Fimbel R., Oesterhelt G., Lehmann M., van Loon A.P.G.M.
Appl. Environ. Microbiol. 65:367-373(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59805 Genomic DNA. Translation: AAB52507.1.

3D structure databases

ProteinModelPortalO00085.
SMRO00085. Positions 31-466.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.1.3.8. 536.

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 namePHYA1_ASPTE
AccessionPrimary (citable) accession number: O00085
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 63 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