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O00092

- PHYA_ASPFU

UniProt

O00092 - PHYA_ASPFU

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
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    • History
      Entry version 103 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
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    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

    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-SubCell

    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 – 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.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO00092.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Curated

    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

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    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

    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