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O66037

- PHYT_BACSD

UniProt

O66037 - PHYT_BACSD

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Protein

3-phytase

Gene

phy

Organism
Bacillus sp. (strain DS11)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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-KW
Complete GO annotation...

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA
60 70 80 90 100
GDAADDPAIW LDPKNPQNSK LITTNKKSGL AVYSLEGKML HSYHTGKLNN
110 120 130 140 150
VDIRYDFPLN GKKVDIAAAS NRSEGKNTIE IYAIDGKNGT LQSITDPNRP
160 170 180 190 200
IASAIDEVYG FSLYHSQKTG KYYAMVTGKE GEFEQYELNA DKNGYISGKK
210 220 230 240 250
VRAFKMNSQT EGMAADDEYG SLYIAEEDEA IWKFSAEPDG GSNGTVIDRA
260 270 280 290 300
DGRHLTPDIE GLTIYYAADG KGYLLASSQG NSSYAIYERQ GQNKYVADFQ
310 320 330 340 350
ITDGPETDGT SDTDGIDVLG FGLGPEYPFG LFVAQDGENI DHGQKANQNF
360 370 380
KMVPWERIAD KIGFHPQVNK QVDPRKMTDR SGK
Length:383
Mass (Da):41,802
Last modified:August 1, 1998 - v1
Checksum:iDCB65188F7B61C8C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85968 Genomic DNA. Translation: AAC38573.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U85968 Genomic DNA. Translation: AAC38573.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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: November 26, 2014
This is version 70 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