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O00092

- PHYA_ASPFU

UniProt

O00092 - PHYA_ASPFU

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Protein

3-phytase A

Gene

phyA

Organism
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of inorganic orthophosphate from phytate.

Catalytic activityi

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

pH dependencei

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

Temperature dependencei

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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei81 – 811NucleophileBy similarity
Active sitei360 – 3601Proton donorBy similarity

GO - Molecular functioni

  1. 3-phytase activity Source: ASPGD
  2. 4-phytase activity Source: ASPGD
  3. acid phosphatase activity Source: InterPro

GO - Biological processi

  1. dephosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Enzyme and pathway databases

BRENDAi3.1.3.8. 508.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:phyA
Synonyms:phyA3
ORF Names:AFUA_4G08630
OrganismiNeosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) (Aspergillus fumigatus)
Taxonomic identifieri330879 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus
ProteomesiUP000002530: Chromosome 4

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 26261 PublicationAdd
BLAST
Chaini27 – 4654393-phytase APRO_0000023969Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi30 ↔ 391 Publication
Disulfide bondi70 ↔ 4121 Publication
Glycosylationi104 – 1041N-linked (GlcNAc...)
Glycosylationi119 – 1191N-linked (GlcNAc...)Sequence Analysis
Glycosylationi205 – 2051N-linked (GlcNAc...)
Disulfide bondi213 ↔ 4631 Publication
Glycosylationi228 – 2281N-linked (GlcNAc...)
Disulfide bondi262 ↔ 2801 Publication
Glycosylationi337 – 3371N-linked (GlcNAc...)
Glycosylationi350 – 3501N-linked (GlcNAc...)
Glycosylationi374 – 3741N-linked (GlcNAc...)
Disulfide bondi434 ↔ 4421 Publication

Keywords - PTMi

Disulfide bond, Glycoprotein

Structurei

Secondary structure

1
465
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni33 – 353Combined sources
Helixi41 – 444Combined sources
Helixi48 – 503Combined sources
Turni57 – 604Combined sources
Beta strandi70 – 8011Combined sources
Helixi88 – 10417Combined sources
Helixi110 – 1167Combined sources
Beta strandi124 – 1274Combined sources
Helixi129 – 14517Combined sources
Helixi147 – 1504Combined sources
Beta strandi156 – 1616Combined sources
Helixi163 – 18119Combined sources
Beta strandi194 – 1985Combined sources
Beta strandi201 – 2044Combined sources
Helixi214 – 2174Combined sources
Helixi221 – 24424Combined sources
Helixi252 – 26918Combined sources
Helixi280 – 2823Combined sources
Helixi285 – 30218Combined sources
Turni308 – 3103Combined sources
Helixi311 – 3144Combined sources
Helixi315 – 32612Combined sources
Beta strandi333 – 3353Combined sources
Helixi338 – 3425Combined sources
Turni344 – 3463Combined sources
Beta strandi352 – 3587Combined sources
Helixi360 – 36910Combined sources
Turni370 – 3756Combined sources
Beta strandi381 – 3833Combined sources
Helixi387 – 3904Combined sources
Helixi395 – 3984Combined sources
Beta strandi404 – 4129Combined sources
Beta strandi419 – 4246Combined sources
Beta strandi432 – 4343Combined sources
Helixi444 – 4507Combined sources
Helixi452 – 4565Combined sources
Turni457 – 4593Combined sources
Helixi460 – 4634Combined sources

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QWOX-ray1.50A24-465[»]
1SK8X-ray1.65A27-464[»]
1SK9X-ray1.64A27-464[»]
1SKAX-ray1.69A27-464[»]
1SKBX-ray1.58A27-464[»]
ProteinModelPortaliO00092.
SMRiO00092. Positions 30-464.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO00092.

Family & Domainsi

Sequence similaritiesi

Belongs to the histidine acid phosphatase family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG260296.
HOGENOMiHOG000189493.
InParanoidiO00092.
KOiK01083.
OMAiWAQYSPY.
OrthoDBiEOG7QC85C.

Family and domain databases

Gene3Di3.40.50.1240. 1 hit.
InterProiIPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view]
PfamiPF00328. His_Phos_2. 1 hit.
[Graphical view]
PIRSFiPIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMiSSF53254. SSF53254. 1 hit.
PROSITEiPS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

O00092-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MVTLTFLLSA AYLLSGRVSA APSSAGSKSC DTVDLGYQCS PATSHLWGQY
60 70 80 90 100
SPFFSLEDEL SVSSKLPKDC RITLVQVLSR HGARYPTSSK SKKYKKLVTA
110 120 130 140 150
IQANATDFKG KFAFLKTYNY TLGADDLTPF GEQQLVNSGI KFYQRYKALA
160 170 180 190 200
RSVVPFIRAS GSDRVIASGE KFIEGFQQAK LADPGATNRA APAISVIIPE
210 220 230 240 250
SETFNNTLDH GVCTKFEASQ LGDEVAANFT ALFAPDIRAR AEKHLPGVTL
260 270 280 290 300
TDEDVVSLMD MCSFDTVART SDASQLSPFC QLFTHNEWKK YNYLQSLGKY
310 320 330 340 350
YGYGAGNPLG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL VSNPATFPLN
360 370 380 390 400
ATMYVDFSHD NSMVSIFFAL GLYNGTEPLS RTSVESAKEL DGYSASWVVP
410 420 430 440 450
FGARAYFETM QCKSEKEPLV RALINDRVVP LHGCDVDKLG RCKLNDFVKG
460
LSWARSGGNW GECFS
Length:465
Mass (Da):50,836
Last modified:July 1, 1997 - v1
Checksum:i86FC1D9058C9B2C9
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59804 Genomic DNA. Translation: AAB96872.1.
AAHF01000005 Genomic DNA. Translation: EAL89926.2. Different initiation.
AJ419776 Genomic DNA. Translation: CAD12029.1.
RefSeqiXP_751964.2. XM_746871.2.

Genome annotation databases

GeneIDi3509324.
KEGGiafm:AFUA_4G08630.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U59804 Genomic DNA. Translation: AAB96872.1 .
AAHF01000005 Genomic DNA. Translation: EAL89926.2 . Different initiation.
AJ419776 Genomic DNA. Translation: CAD12029.1 .
RefSeqi XP_751964.2. XM_746871.2.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1QWO X-ray 1.50 A 24-465 [» ]
1SK8 X-ray 1.65 A 27-464 [» ]
1SK9 X-ray 1.64 A 27-464 [» ]
1SKA X-ray 1.69 A 27-464 [» ]
1SKB X-ray 1.58 A 27-464 [» ]
ProteinModelPortali O00092.
SMRi O00092. Positions 30-464.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 3509324.
KEGGi afm:AFUA_4G08630.

Phylogenomic databases

eggNOGi NOG260296.
HOGENOMi HOG000189493.
InParanoidi O00092.
KOi K01083.
OMAi WAQYSPY.
OrthoDBi EOG7QC85C.

Enzyme and pathway databases

BRENDAi 3.1.3.8. 508.

Miscellaneous databases

EvolutionaryTracei O00092.

Family and domain databases

Gene3Di 3.40.50.1240. 1 hit.
InterProi IPR000560. His_Pase_superF_clade-2.
IPR029033. His_PPase_superfam.
IPR016274. Histidine_acid_Pase_euk.
[Graphical view ]
Pfami PF00328. His_Phos_2. 1 hit.
[Graphical view ]
PIRSFi PIRSF000894. Acid_phosphatase. 1 hit.
SUPFAMi SSF53254. SSF53254. 1 hit.
PROSITEi PS00616. HIS_ACID_PHOSPHAT_1. 1 hit.
PS00778. HIS_ACID_PHOSPHAT_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.

Entry informationi

Entry nameiPHYA_ASPFU
AccessioniPrimary (citable) accession number: O00092
Secondary accession number(s): Q4WPA8, Q8WZJ5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: July 1, 1997
Last modified: October 29, 2014
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3