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P34753

- PHYA_ASPAW

UniProt

P34753 - PHYA_ASPAW

Protein

3-phytase A

Gene

phyA

Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi
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    • History
      Entry version 72 (01 Oct 2014)
      Sequence version 1 (01 Feb 1994)
      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.

    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

    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:phy
    OrganismiAspergillus awamori (Black koji mold)
    Taxonomic identifieri105351 [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 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 4674443-phytase APRO_0000023971Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi27 – 271N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi31 ↔ 40By similarity
    Glycosylationi59 – 591N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi71 ↔ 414By similarity
    Glycosylationi105 – 1051N-linked (GlcNAc...)Sequence Analysis
    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
    Glycosylationi388 – 3881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi436 ↔ 444By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliP34753.
    SMRiP34753. Positions 30-467.
    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.

    P34753-1 [UniParc]FASTAAdd to Basket

    « Hide

    MGVSAVLLPL YLLAGVTSGL AVPASRNQST CDTVDQGYQC FSETSHLWGQ    50
    YAPFFSLANE SAISPDVPAG CRVTFAQVLS RHGARYPTES KGKKYSALIE 100
    EIQQNVTTFD GKYAFLKTYN YSLGADDLTP FGEQELVNSG IKFYQRYESL 150
    TRNIIPFIRS SGSSRVIASG EKFIEGFQST KLKDPRAQPG QSSPKIDVVI 200
    SEASSSNNTL DPGTCTVFED SELADTVEAN FTATFAPSIR QRLENDLSGV 250
    TLTDTEVTYL MDMCSFDTIS TSTVDTKLSP FCDLFTHDEW IHYDYLQSLK 300
    KYYGHGAGNP LGPTQGVGYA NELIARLTHS PVHDDTSSNH TLDSNPATFP 350
    LNSTLYADFS HDNGIISILF ALGLYNGTKP LSTTTVENIT QTDGFSSAWT 400
    VPFASRLYVE MMQCQAEQEP LVRVLVNDRV VPLHGCPIDA LGRCTRDSFV 450
    RGLSFARSGG DWAECSA 467
    Length:467
    Mass (Da):51,075
    Last modified:February 1, 1994 - v1
    Checksum:i118E828A5D7EC661
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02421 Unassigned DNA. Translation: AAA16898.1.
    PIRiJN0889.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02421 Unassigned DNA. Translation: AAA16898.1 .
    PIRi JN0889.

    3D structure databases

    ProteinModelPortali P34753.
    SMRi P34753. Positions 30-467.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    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 cloning and sequencing of the genes encoding phytase (phy) and pH 2.5-optimum acid phosphatase (aph) from Aspergillus niger var. awamori."
      Piddington C.S., Houston C.S., Paloheimo M.T., Cantrell M.A., Miettinen-Oinonen A., Nevalainen H., Rambosek J.A.
      Gene 133:55-62(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: ALK0243.

    Entry informationi

    Entry nameiPHYA_ASPAW
    AccessioniPrimary (citable) accession number: P34753
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: October 1, 2014
    This is version 72 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Documents

    1. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3