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O00100 (PHYA2_ASPTE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 11, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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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 lineageEukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus

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 By similarity.

Sequence similarities

Belongs to the histidine acid phosphatase family.

Biophysicochemical properties

Kinetic parameters:

KM=23.2 µM for phytate Ref.3

pH dependence:

Optimum pH is 5.5. Active from 4 to 6.5.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionHydrolase
   PTMDisulfide bond
Glycoprotein
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processdephosphorylation

Inferred from electronic annotation. Source: GOC

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_function3-phytase activity

Inferred from electronic annotation. Source: 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 Ref.2
Chain20 – 4664473-phytase A
PRO_0000283712

Sites

Active site821Nucleophile By similarity
Active site3621Proton donor By similarity

Amino acid modifications

Glycosylation271N-linked (GlcNAc...) Potential
Glycosylation1051N-linked (GlcNAc...) Potential
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
O00100 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: F2AECEC1AF7C22C4

FASTA46651,055
        10         20         30         40         50         60 
MGVFVVLLSI ATLFGSTSGT ALGPRGNHSD CTSVDRGYQC FPELSHKWGL YAPYFSLQDE 

        70         80         90        100        110        120 
SPFPLDVPDD CHITFVQVLA RHGARSPTDS KTKAYAATIA AIQKNATALP GKYAFLKSYN 

       130        140        150        160        170        180 
YSMGSENLNP FGRNQLQDLG AQFYRRYDTL TRHINPFVRA ADSSRVHESA EKFVEGFQNA 

       190        200        210        220        230        240 
RQGDPHANPH QPSPRVDVVI PEGTAYNNTL EHSICTAFEA STVGDAAADN FTAVFAPAIA 

       250        260        270        280        290        300 
KRLEADLPGV QLSADDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTAAEW TQYNYLLSLD 

       310        320        330        340        350        360 
KYYGYGGGNP LGPVQGVGWA NELIARLTRS PVHDHTCVNN TLDANPATFP LNATLYADFS 

       370        380        390        400        410        420 
HDSNLVSIFW ALGLYNGTKP LSQTTVEDIT RTDGYAAAWT VPFAARAYIE MMQCRAEKQP 

       430        440        450        460 
LVRVLVNDRV MPLHGCAVDN LGRCKRDDFV EGLSFARAGG NWAECF

« Hide

References

[1]"Cloning of the phytases of Aspergillus nidulans and Talaromyces thermophilus and their evolutionary relation to other histidine acid phosphatases."
Pasamontes L., Haiker M., Henriquez Huecas M., Hug D., Mitchell D.B., Broger C., van Loon A.P.
Submitted (JUN-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI 44243.
[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 20-35, SUBUNIT.
Strain: ATCC 10020 / NRRL 1960 / CBS 116.46 / IFO 6123 / DSM 826 / IMI 44243.
[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		U60412 Genomic DNA. Translation: AAB58465.1.

3D structure databases

HSSPHSSP built from PDB template 1IHP based on UniProtKB P34752.
ProteinModelPortalO00100.
SMRO00100. Positions 31-466.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG319987.
HOGENOMHOG000189493.

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 namePHYA2_ASPTE
AccessionPrimary (citable) accession number: O00100
Entry history
Integrated into UniProtKB/Swiss-Prot: April 17, 2007
Last sequence update: July 1, 1997
Last modified: July 11, 2012
This is version 54 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

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