Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(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)

O00085

- PHYA1_ASPTE

UniProt

O00085 - PHYA1_ASPTE

Protein

3-phytase A

Gene

phyA

Organism
Aspergillus terreus
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 65 (01 Oct 2014)
      Sequence version 1 (01 Jul 1997)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.1 Publication

    Catalytic activityi

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

    Kineticsi

    1. KM=10.6 µM for phytate1 Publication

    pH dependencei

    Optimum pH is 5.5. Active from 2.5 to 7.5 with phytic acid as substrate. The optimum pH is shifted to more acidic values with 4-nitrophenyl phosphate as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei82 – 821NucleophileBy similarity
    Active sitei362 – 3621Proton donorBy similarity

    GO - Molecular functioni

    1. 3-phytase activity Source: UniProtKB-EC
    2. acid phosphatase activity Source: InterPro

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BRENDAi3.1.3.8. 536.

    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
    OrganismiAspergillus terreus
    Taxonomic identifieri33178 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    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 – 1919By similarityAdd
    BLAST
    Chaini20 – 4664473-phytase APRO_0000023972Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi31 ↔ 40By similarity
    Disulfide bondi71 ↔ 414By similarity
    Glycosylationi120 – 1201N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi207 – 2071N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi215 ↔ 465By similarity
    Glycosylationi230 – 2301N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi264 ↔ 282By similarity
    Glycosylationi339 – 3391N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi352 – 3521N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi376 – 3761N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi436 ↔ 444By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO00085.
    SMRiO00085. Positions 31-466.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Curated

    Keywords - Domaini

    Signal

    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.

    O00085-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGFLAIVLSV ALLFRSTSGT PLGPRGKHSD CNSVDHGYQC FPELSHKWGL    50
    YAPYFSLQDE SPFPLDVPED CHITFVQVLA RHGARSPTHS KTKAYAATIA 100
    AIQKSATAFP GKYAFLQSYN YSLDSEELTP FGRNQLRDLG AQFYERYNAL 150
    TRHINPFVRA TDASRVHESA EKFVEGFQTA RQDDHHANPH QPSPRVDVAI 200
    PEGSAYNNTL EHSLCTAFES STVGDDAVAN FTAVFAPAIA QRLEADLPGV 250
    QLSTDDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTATEW TQYNYLLSLD 300
    KYYGYGGGNP LGPVQGVGWA NELMARLTRA PVHDHTCVNN TLDASPATFP 350
    LNATLYADFS HDSNLVSIFW ALGLYNGTAP LSQTSVESVS QTDGYAAAWT 400
    VPFAARAYVE MMQCRAEKEP LVRVLVNDRV MPLHGCPTDK LGRCKRDAFV 450
    AGLSFAQAGG NWADCF 466
    Length:466
    Mass (Da):51,093
    Last modified:July 1, 1997 - v1
    Checksum:i21CDCB559C96AE66
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59805 Genomic DNA. Translation: AAB52507.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59805 Genomic DNA. Translation: AAB52507.1 .

    3D structure databases

    ProteinModelPortali O00085.
    SMRi O00085. Positions 31-466.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    BRENDAi 3.1.3.8. 536.

    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. "The phytase subfamily of histidine acid phosphatases: isolation of genes for two novel phytases from the fungi Aspergillus terreus and Myceliophthora thermophila."
      Mitchell D.B., Vogel K., Weimann B.J., Pasamontes L., van Loon A.P.G.M.
      Microbiology 143:245-252(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
      Strain: 9A1.
    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 29-38 AND 192-200, SUBUNIT.
      Strain: 9A1.
    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.

    Entry informationi

    Entry nameiPHYA1_ASPTE
    AccessioniPrimary (citable) accession number: O00085
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 65 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

    Direct protein sequencing

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3