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O66037

- PHYT_BACSD

UniProt

O66037 - PHYT_BACSD

Protein

3-phytase

Gene

phy

Organism
Bacillus sp. (strain DS11)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 68 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    GO - Molecular functioni

    1. 3-phytase activity Source: UniProtKB-EC

    Keywords - Molecular functioni

    Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    3-phytase (EC:3.1.3.8)
    Alternative name(s):
    Myo-inositol-hexaphosphate 3-phosphohydrolase
    Phytate 3-phosphatase
    Gene namesi
    Name:phy
    OrganismiBacillus sp. (strain DS11)
    Taxonomic identifieri86035 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

    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 – 2626Sequence AnalysisAdd
    BLAST
    Propeptidei27 – 3041 PublicationPRO_0000022058
    Chaini31 – 3833533-phytasePRO_0000022059Add
    BLAST

    Structurei

    Secondary structure

    1
    383
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi35 – 384
    Beta strandi41 – 433
    Beta strandi54 – 607
    Helixi66 – 683
    Beta strandi70 – 756
    Beta strandi81 – 844
    Beta strandi89 – 924
    Beta strandi98 – 10912
    Beta strandi112 – 12110
    Turni124 – 1263
    Beta strandi128 – 1358
    Turni136 – 1394
    Beta strandi140 – 1434
    Beta strandi147 – 1493
    Beta strandi154 – 1574
    Beta strandi161 – 1655
    Turni167 – 1693
    Beta strandi172 – 1776
    Beta strandi179 – 19012
    Beta strandi194 – 20512
    Beta strandi210 – 2167
    Turni217 – 2204
    Beta strandi221 – 2266
    Turni227 – 2293
    Beta strandi230 – 2378
    Helixi238 – 2403
    Beta strandi245 – 2495
    Beta strandi251 – 2544
    Beta strandi259 – 2668
    Helixi268 – 2703
    Beta strandi272 – 2787
    Helixi279 – 2813
    Beta strandi283 – 2908
    Beta strandi295 – 3017
    Beta strandi305 – 3073
    Beta strandi316 – 3194
    Beta strandi324 – 3263
    Beta strandi331 – 3388
    Beta strandi344 – 3463
    Beta strandi349 – 3546
    Helixi356 – 3594
    Helixi360 – 3623
    Helixi374 – 3763

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CVMX-ray2.40A29-381[»]
    1H6LX-ray1.80A29-381[»]
    1POOX-ray2.10A29-383[»]
    1QLGX-ray2.20A29-381[»]
    2POOX-ray2.05A29-383[»]
    ProteinModelPortaliO66037.
    SMRiO66037. Positions 29-381.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO66037.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini31 – 362332BPPPROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 BPP (beta-propeller phytase) domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di2.120.10.20. 1 hit.
    InterProiIPR003431. b_Phytase.
    [Graphical view]
    PfamiPF02333. Phytase. 1 hit.
    [Graphical view]
    PROSITEiPS51662. BP_PHYTASE. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    O66037-1 [UniParc]FASTAAdd to Basket

    « Hide

    MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA    50
    GDAADDPAIW LDPKNPQNSK LITTNKKSGL AVYSLEGKML HSYHTGKLNN 100
    VDIRYDFPLN GKKVDIAAAS NRSEGKNTIE IYAIDGKNGT LQSITDPNRP 150
    IASAIDEVYG FSLYHSQKTG KYYAMVTGKE GEFEQYELNA DKNGYISGKK 200
    VRAFKMNSQT EGMAADDEYG SLYIAEEDEA IWKFSAEPDG GSNGTVIDRA 250
    DGRHLTPDIE GLTIYYAADG KGYLLASSQG NSSYAIYERQ GQNKYVADFQ 300
    ITDGPETDGT SDTDGIDVLG FGLGPEYPFG LFVAQDGENI DHGQKANQNF 350
    KMVPWERIAD KIGFHPQVNK QVDPRKMTDR SGK 383
    Length:383
    Mass (Da):41,802
    Last modified:August 1, 1998 - v1
    Checksum:iDCB65188F7B61C8C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85968 Genomic DNA. Translation: AAC38573.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U85968 Genomic DNA. Translation: AAC38573.1 .

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CVM X-ray 2.40 A 29-381 [» ]
    1H6L X-ray 1.80 A 29-381 [» ]
    1POO X-ray 2.10 A 29-383 [» ]
    1QLG X-ray 2.20 A 29-381 [» ]
    2POO X-ray 2.05 A 29-383 [» ]
    ProteinModelPortali O66037.
    SMRi O66037. Positions 29-381.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Miscellaneous databases

    EvolutionaryTracei O66037.

    Family and domain databases

    Gene3Di 2.120.10.20. 1 hit.
    InterProi IPR003431. b_Phytase.
    [Graphical view ]
    Pfami PF02333. Phytase. 1 hit.
    [Graphical view ]
    PROSITEi PS51662. BP_PHYTASE. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning of the thermostable phytase gene (phy) from Bacillus sp. DS11 and its overexpression in Escherichia coli."
      Kim Y.-O., Lee J.-K., Kim H.-K., Yu J.-H., Oh T.-K.
      FEMS Microbiol. Lett. 162:185-191(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 31-44 AND 214-223.
    2. "Preliminary X-ray crystallographic analysis of a novel phytase from a Bacillus amyloliquefaciens strain."
      Ha N.-C., Kim Y.-O., Oh T.-K., Oh B.-H.
      Acta Crystallogr. D 55:691-693(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
    3. "Crystal structures of a novel, thermostable phytase in partially and fully calcium-loaded states."
      Ha N.-C., Oh B.-C., Shin S., Kim H.-J., Oh T.-K., Kim Y.-O., Choi K.Y., Oh B.-H.
      Nat. Struct. Biol. 7:147-153(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).

    Entry informationi

    Entry nameiPHYT_BACSD
    AccessioniPrimary (citable) accession number: O66037
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 15, 1998
    Last sequence update: August 1, 1998
    Last modified: October 1, 2014
    This is version 68 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    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