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O00107

- PHYA_THIHE

UniProt

O00107 - PHYA_THIHE

Protein

3-phytase A

Gene

PHYA

Organism
Thielavia heterothallica (Myceliophthora thermophila)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 64 (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

    Optimum pH is 5.5-6.0. Active from 3.5 to 8.5 with phytic acid as substrate. The optimum pH is shifted to more acidic values with 4-nitrophenyl phosphate as substrate.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei75 – 751NucleophileBy similarity
    Active sitei369 – 3691Proton 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
    OrganismiThielavia heterothallica (Myceliophthora thermophila)
    Taxonomic identifieri78579 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesSordariomycetidaeSordarialesChaetomiaceaeMyceliophthora

    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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 4874683-phytase APRO_0000023973Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi26 ↔ 35By similarity
    Disulfide bondi64 ↔ 421By similarity
    Glycosylationi165 – 1651N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi200 – 2001N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi208 ↔ 485By similarity
    Glycosylationi247 – 2471N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi260 ↔ 289By similarity
    Glycosylationi346 – 3461N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi456 ↔ 464By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Structurei

    3D structure databases

    ProteinModelPortaliO00107.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi423 – 43311Poly-GlyAdd
    BLAST

    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.

    O00107-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTGLGVMVVM VGFLAIASLQ SESRPCDTPD LGFQCGTAIS HFWGQYSPYF    50
    SVPSELDASI PDDCEVTFAQ VLSRHGARAP TLKRAASYVD LIDRIHHGAI 100
    SYGPGYEFLR TYDYTLGADE LTRTGQQQMV NSGIKFYRRY RALARKSIPF 150
    VRTAGQDRVV HSAENFTQGF HSALLADRGS TVRPTLPYDM VVIPETAGAN 200
    NTLHNDLCTA FEEGPYSTIG DDAQDTYLST FAGPITARVN ANLPGANLTD 250
    ADTVALMDLC PFETVASSSS DPATADAGGG NGRPLSPFCR LFSESEWRAY 300
    DYLQSVGKWY GYGPGNPLGP TQGVGFVNEL LARLAGVPVR DGTSTNRTLD 350
    GDPRTFPLGR PLYADFSHDN DMMGVLGALG AYDGVPPLDK TARRDPEELG 400
    GYAASWAVPF AARIYVEKMR CSGGGGGGGG GEGRQEKDEE MVRVLVNDRV 450
    MTLKGCGADE RGMCTLERFI ESMAFARGNG KWDLCFA 487
    Length:487
    Mass (Da):52,538
    Last modified:July 1, 1997 - v1
    Checksum:i97D10EDC83D051DB
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59806 Genomic DNA. Translation: AAB52508.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U59806 Genomic DNA. Translation: AAB52508.1 .

    3D structure databases

    ProteinModelPortali O00107.
    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 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.

    Entry informationi

    Entry nameiPHYA_THIHE
    AccessioniPrimary (citable) accession number: O00107
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 16, 2004
    Last sequence update: July 1, 1997
    Last modified: October 1, 2014
    This is version 64 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