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P34755

- PHYB_ASPAW

UniProt

P34755 - PHYB_ASPAW

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Protein
3-phytase B
Gene
phyB, aph
Organism
Aspergillus awamori (Black koji mold)
Status
Reviewed - Annotation score: 4 out of 5 - Experimental evidence at protein leveli

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 – 821Nucleophile
Active sitei338 – 3381Proton donor

GO - Molecular functioni

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

GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phytase B (EC:3.1.3.8)
    Alternative name(s):
    Myo-inositol-hexaphosphate 3-phosphohydrolase B
    pH 2.5 optimum acid phosphatase
    Gene namesi
    Name:phyB
    Synonyms:aph
    OrganismiAspergillus awamori (Black koji mold)
    Taxonomic identifieri105351 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1919 By similarity
    Add
    BLAST
    Chaini20 – 4794603-phytase B
    PRO_0000023975Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi71 ↔ 387
    Disulfide bondi128 ↔ 472
    Glycosylationi191 – 1911N-linked (GlcNAc...)
    Disulfide bondi216 ↔ 441
    Disulfide bondi225 ↔ 298
    Glycosylationi315 – 3151N-linked (GlcNAc...)
    Disulfide bondi413 ↔ 421
    Glycosylationi458 – 4581N-linked (GlcNAc...)

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Homodimer.

    Structurei

    Secondary structure

    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi41 – 433
    Helixi45 – 473
    Beta strandi71 – 8111
    Helixi89 – 10315
    Helixi112 – 1198
    Helixi127 – 1293
    Helixi141 – 15616
    Helixi157 – 1593
    Beta strandi162 – 1643
    Beta strandi166 – 1738
    Helixi174 – 18815
    Helixi189 – 1913
    Helixi192 – 1954
    Beta strandi196 – 2016
    Helixi205 – 2073
    Beta strandi210 – 2134
    Turni224 – 2274
    Helixi234 – 24512
    Helixi253 – 26614
    Turni267 – 2693
    Helixi276 – 2783
    Helixi281 – 29818
    Helixi306 – 32318
    Helixi325 – 3284
    Beta strandi330 – 3367
    Helixi338 – 34811
    Beta strandi359 – 3613
    Helixi370 – 3723
    Beta strandi379 – 3879
    Beta strandi395 – 4039
    Beta strandi406 – 4083
    Helixi417 – 4193
    Helixi423 – 43311
    Helixi437 – 4404
    Turni453 – 4553

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1QFXX-ray2.40A/B20-479[»]
    ProteinModelPortaliP34755.
    SMRiP34755. Positions 33-479.

    Miscellaneous databases

    EvolutionaryTraceiP34755.

    Family & Domainsi

    Sequence similaritiesi

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.40.50.1240. 3 hits.
    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.

    P34755-1 [UniParc]FASTAAdd to Basket

    « Hide

    MPRTSLLTLA CALATGASAF SYGAAIPQST QEKQFSQEFR DGYSILKHYG    50
    GNGPYSERVS YGIARDPPTS CEVDQVIMVK RHGERYPSPS AGKDIEEALA 100
    KVYSINTTEY KGDLAFLNDW TYYVPNECYY NAETTSGPYA GLLDAYNHGN 150
    DYKARYGHLW NGETVVPFFS SGYGRVIETA RKFGEGFFGY NYSTNAALNI 200
    ISESEVMGAD SLTPTCDTDN DQTTCDNLTY QLPQFKVAAA RLNSQNPGMN 250
    LTASDVYNLM VMASFELNAR PFSNWINAFT QDEWVSFGYV EDLNYYYCAG 300
    PGDKNMAAVG AVYANASLTL LNQGPKEAGS LFFNFAHDTN ITPILAALGV 350
    LIPNEDLPLD RVAFGNPYSI GNIVPMGGHL TIERLSCQAT ALSDEGTYVR 400
    LVLNEAVLPF NDCTSGPGYS CPLANYTSIL NKNLPDYTTT CNVSASYPQY 450
    LSFWWNYNTT TELNYRSSPI ACQEGDAMD 479
    Length:479
    Mass (Da):52,678
    Last modified:February 1, 1994 - v1
    Checksum:i4F8E0F3778CC3B08
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02420 Unassigned DNA. Translation: AAA16897.1.
    PIRiJN0890.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L02420 Unassigned DNA. Translation: AAA16897.1 .
    PIRi JN0890.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1QFX X-ray 2.40 A/B 20-479 [» ]
    ProteinModelPortali P34755.
    SMRi P34755. Positions 33-479.
    ModBasei Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei P34755.

    Family and domain databases

    Gene3Di 3.40.50.1240. 3 hits.
    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.
    2. "Crystal structure of Aspergillus niger pH 2.5 acid phosphatase at 2.4-A resolution."
      Kostrewa D., Wyss M., D'Arcy A., van Loon A.P.G.M.
      J. Mol. Biol. 288:965-974(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS).

    Entry informationi

    Entry nameiPHYB_ASPAW
    AccessioniPrimary (citable) accession number: P34755
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 1994
    Last sequence update: February 1, 1994
    Last modified: June 11, 2014
    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

    3D-structure

    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

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