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O00092 (PHYA_ASPFU) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 102. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Synonyms:phyA3
ORF Names:AFUA_4G08630
OrganismNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus) [Reference proteome]
Taxonomic identifier330879 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length465 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:

Highly active from pH 3 to 5 with 4-nitrophenyl phosphate as substrate, and from 2.5 to 7.5 with phytic acid.

Temperature dependence:

Able to withstand temperatures up to 100 degrees Celsius over a period of 20 min, with a loss of only 10% of the initial enzymatic activity.

Sequence caution

The sequence EAL89926.2 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2626 Ref.1
Chain27 – 4654393-phytase A
PRO_0000023969

Sites

Active site811Nucleophile By similarity
Active site3601Proton donor By similarity

Amino acid modifications

Glycosylation1041N-linked (GlcNAc...)
Glycosylation1191N-linked (GlcNAc...) Potential
Glycosylation2051N-linked (GlcNAc...)
Glycosylation2281N-linked (GlcNAc...)
Glycosylation3371N-linked (GlcNAc...)
Glycosylation3501N-linked (GlcNAc...)
Glycosylation3741N-linked (GlcNAc...)
Disulfide bond30 ↔ 39 Ref.4
Disulfide bond70 ↔ 412 Ref.4
Disulfide bond213 ↔ 463 Ref.4
Disulfide bond262 ↔ 280 Ref.4
Disulfide bond434 ↔ 442 Ref.4

Secondary structure

........................................................................ 465
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O00092 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 86FC1D9058C9B2C9

FASTA46550,836
        10         20         30         40         50         60 
MVTLTFLLSA AYLLSGRVSA APSSAGSKSC DTVDLGYQCS PATSHLWGQY SPFFSLEDEL 

        70         80         90        100        110        120 
SVSSKLPKDC RITLVQVLSR HGARYPTSSK SKKYKKLVTA IQANATDFKG KFAFLKTYNY 

       130        140        150        160        170        180 
TLGADDLTPF GEQQLVNSGI KFYQRYKALA RSVVPFIRAS GSDRVIASGE KFIEGFQQAK 

       190        200        210        220        230        240 
LADPGATNRA APAISVIIPE SETFNNTLDH GVCTKFEASQ LGDEVAANFT ALFAPDIRAR 

       250        260        270        280        290        300 
AEKHLPGVTL TDEDVVSLMD MCSFDTVART SDASQLSPFC QLFTHNEWKK YNYLQSLGKY 

       310        320        330        340        350        360 
YGYGAGNPLG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL VSNPATFPLN ATMYVDFSHD 

       370        380        390        400        410        420 
NSMVSIFFAL GLYNGTEPLS RTSVESAKEL DGYSASWVVP FGARAYFETM QCKSEKEPLV 

       430        440        450        460 
RALINDRVVP LHGCDVDKLG RCKLNDFVKG LSWARSGGNW GECFS 

« Hide

References

« Hide 'large scale' references
[1]"Gene cloning, purification, and characterization of a heat-stable phytase from the fungus Aspergillus fumigatus."
Pasamontes L., Haiker M., Wyss M., Tessier M., van Loon A.P.G.M.
Appl. Environ. Microbiol. 63:1696-1700(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 27-37, CHARACTERIZATION.
Strain: ATCC 34625 / CS-270.
[2]"Genomic sequence of the pathogenic and allergenic filamentous fungus Aspergillus fumigatus."
Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J., Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P., Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L. expand/collapse author list , Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N., Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K., Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E., Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A., Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D., O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R., Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.G., Denning D.W.
Nature 438:1151-1156(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100.
[3]"Cloning of phytase gene from Aspergillus fumigatus and its expression in Pichia pastoris."
Zhang G.
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 24-465.
Strain: CCTCC AF93024.
[4]"Crystallographic snapshots of Aspergillus fumigatus phytase, revealing its enzymatic dynamics."
Liu Q., Huang Q., Lei X.G., Hao Q.
Structure 12:1575-1583(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 27-465, DISULFIDE BONDS.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U59804 Genomic DNA. Translation: AAB96872.1.
AAHF01000005 Genomic DNA. Translation: EAL89926.2. Different initiation.
AJ419776 Genomic DNA. Translation: CAD12029.1.
RefSeqXP_751964.2. XM_746871.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWOX-ray1.50A24-465[»]
1SK8X-ray1.65A27-464[»]
1SK9X-ray1.64A27-464[»]
1SKAX-ray1.69A27-464[»]
1SKBX-ray1.58A27-464[»]
ProteinModelPortalO00092.
SMRO00092. Positions 30-464.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3509324.
KEGGafm:AFUA_4G08630.

Phylogenomic databases

eggNOGNOG260296.
HOGENOMHOG000189493.
KOK01083.
OMAWAQYSPY.
OrthoDBEOG7QC85C.

Enzyme and pathway databases

BRENDA3.1.3.8. 508.

Family and domain databases

Gene3D3.40.50.1240. 1 hit.
InterProIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMSSF53254. SSF53254. 1 hit.
PROSITEPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO00092.

Entry information

Entry namePHYA_ASPFU
AccessionPrimary (citable) accession number: O00092
Secondary accession number(s): Q4WPA8, Q8WZJ5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: June 11, 2014
This is version 102 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references