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Protein

3-phytase A

Gene

phyA

Organism
Aspergillus terreus
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

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)DescriptionActionsGraphical viewLength
    Active sitei82NucleophileBy similarity1
    Active sitei362Proton donorBy similarity1

    GO - Molecular functioni

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Enzyme and pathway databases

    BRENDAi3.1.3.26. 536.
    3.1.3.8. 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

    Complete GO annotation...

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Signal peptidei1 – 19By similarityAdd BLAST19
    ChainiPRO_000002397220 – 4663-phytase AAdd BLAST447

    Amino acid modifications

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Disulfide bondi31 ↔ 40By similarity
    Disulfide bondi71 ↔ 414By similarity
    Glycosylationi120N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi207N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi215 ↔ 465By similarity
    Glycosylationi230N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi264 ↔ 282By similarity
    Glycosylationi339N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi352N-linked (GlcNAc...)Sequence analysis1
    Glycosylationi376N-linked (GlcNAc...)Sequence analysis1
    Disulfide bondi436 ↔ 444By similarity

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.1 Publication

    Structurei

    3D structure databases

    ProteinModelPortaliO00085.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the histidine acid phosphatase family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    CDDicd07061. HP_HAP_like. 1 hit.
    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR033379. Acid_Pase_AS.
    IPR000560. His_Pase_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

            10         20         30         40         50
    MGFLAIVLSV ALLFRSTSGT PLGPRGKHSD CNSVDHGYQC FPELSHKWGL
    60 70 80 90 100
    YAPYFSLQDE SPFPLDVPED CHITFVQVLA RHGARSPTHS KTKAYAATIA
    110 120 130 140 150
    AIQKSATAFP GKYAFLQSYN YSLDSEELTP FGRNQLRDLG AQFYERYNAL
    160 170 180 190 200
    TRHINPFVRA TDASRVHESA EKFVEGFQTA RQDDHHANPH QPSPRVDVAI
    210 220 230 240 250
    PEGSAYNNTL EHSLCTAFES STVGDDAVAN FTAVFAPAIA QRLEADLPGV
    260 270 280 290 300
    QLSTDDVVNL MAMCPFETVS LTDDAHTLSP FCDLFTATEW TQYNYLLSLD
    310 320 330 340 350
    KYYGYGGGNP LGPVQGVGWA NELMARLTRA PVHDHTCVNN TLDASPATFP
    360 370 380 390 400
    LNATLYADFS HDSNLVSIFW ALGLYNGTAP LSQTSVESVS QTDGYAAAWT
    410 420 430 440 450
    VPFAARAYVE MMQCRAEKEP LVRVLVNDRV MPLHGCPTDK LGRCKRDAFV
    460
    AGLSFAQAGG NWADCF
    Length:466
    Mass (Da):51,093
    Last modified:July 1, 1997 - v1
    Checksum:i21CDCB559C96AE66
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U59805 Genomic DNA. Translation: AAB52507.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U59805 Genomic DNA. Translation: AAB52507.1.

    3D structure databases

    ProteinModelPortaliO00085.
    ModBaseiSearch...
    MobiDBiSearch...

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Enzyme and pathway databases

    BRENDAi3.1.3.26. 536.
    3.1.3.8. 536.

    Family and domain databases

    CDDicd07061. HP_HAP_like. 1 hit.
    Gene3Di3.40.50.1240. 1 hit.
    InterProiIPR033379. Acid_Pase_AS.
    IPR000560. His_Pase_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]
    ProtoNetiSearch...

    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 5, 2016
    This is version 73 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

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.