SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O00092

- PHYA_ASPFU

UniProt

O00092 - PHYA_ASPFU

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

3-phytase A

Gene
phyA, phyA3, AFUA_4G08630
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 – 811Nucleophile
Active sitei360 – 3601Proton donor

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

Subcellular locationi

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
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...)
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 – 353
Helixi41 – 444
Helixi48 – 503
Turni57 – 604
Beta strandi70 – 8011
Helixi88 – 10417
Helixi110 – 1167
Beta strandi124 – 1274
Helixi129 – 14517
Helixi147 – 1504
Beta strandi156 – 1616
Helixi163 – 18119
Beta strandi194 – 1985
Beta strandi201 – 2044
Helixi214 – 2174
Helixi221 – 24424
Helixi252 – 26918
Helixi280 – 2823
Helixi285 – 30218
Turni308 – 3103
Helixi311 – 3144
Helixi315 – 32612
Beta strandi333 – 3353
Helixi338 – 3425
Turni344 – 3463
Beta strandi352 – 3587
Helixi360 – 36910
Turni370 – 3756
Beta strandi381 – 3833
Helixi387 – 3904
Helixi395 – 3984
Beta strandi404 – 4129
Beta strandi419 – 4246
Beta strandi432 – 4343
Helixi444 – 4507
Helixi452 – 4565
Turni457 – 4593
Helixi460 – 4634

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.

Miscellaneous databases

EvolutionaryTraceiO00092.

Family & Domainsi

Sequence similaritiesi

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG260296.
HOGENOMiHOG000189493.
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

MVTLTFLLSA AYLLSGRVSA APSSAGSKSC DTVDLGYQCS PATSHLWGQY    50
SPFFSLEDEL SVSSKLPKDC RITLVQVLSR HGARYPTSSK SKKYKKLVTA 100
IQANATDFKG KFAFLKTYNY TLGADDLTPF GEQQLVNSGI KFYQRYKALA 150
RSVVPFIRAS GSDRVIASGE KFIEGFQQAK LADPGATNRA APAISVIIPE 200
SETFNNTLDH GVCTKFEASQ LGDEVAANFT ALFAPDIRAR AEKHLPGVTL 250
TDEDVVSLMD MCSFDTVART SDASQLSPFC QLFTHNEWKK YNYLQSLGKY 300
YGYGAGNPLG PAQGIGFTNE LIARLTRSPV QDHTSTNSTL VSNPATFPLN 350
ATMYVDFSHD NSMVSIFFAL GLYNGTEPLS RTSVESAKEL DGYSASWVVP 400
FGARAYFETM QCKSEKEPLV RALINDRVVP LHGCDVDKLG RCKLNDFVKG 450
LSWARSGGNW GECFS 465
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.
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 1, 2014
This is version 103 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

Similar proteinsi