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O31097

- PHYC_BACIU

UniProt

O31097 - PHYC_BACIU

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Protein

3-phytase

Gene

phyC

Organism
Bacillus subtilis
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli

Functioni

Catalyzes the hydrolysis of inorganic orthophosphate from phytate. Only phytate, ADP, and ATP were hydrolyzed (100, 75, and 50% of the relative activity, respectively).

Catalytic activityi

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

Cofactori

Ca2+Note: Ca(2+) is required for its activity and/or stability.

pH dependencei

Optimum pH is 7.

Temperature dependencei

Optimum temperature is 55 degrees Celsius.

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:phyC
Synonyms:phyB13
OrganismiBacillus subtilis
Taxonomic identifieri1423 [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 – 293PRO_0000022055
Chaini30 – 3833543-phytasePRO_0000022056Add
BLAST

Expressioni

Inductioni

By phytate.

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
Turni76 – 783Combined sources
Beta strandi79 – 846Combined sources
Beta strandi89 – 935Combined sources
Beta strandi98 – 10912Combined sources
Beta strandi112 – 12110Combined sources
Turni124 – 1263Combined sources
Beta strandi128 – 1347Combined sources
Turni136 – 1383Combined sources
Beta strandi141 – 1433Combined sources
Beta strandi161 – 1655Combined sources
Turni167 – 1693Combined sources
Beta strandi172 – 1776Combined sources
Beta strandi179 – 19012Combined sources
Beta strandi196 – 20510Combined sources
Beta strandi210 – 2167Combined sources
Turni217 – 2204Combined sources
Beta strandi221 – 2266Combined sources
Turni227 – 2293Combined sources
Beta strandi230 – 2356Combined sources
Beta strandi245 – 25511Combined 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 strandi331 – 3388Combined sources
Beta strandi349 – 3546Combined sources
Helixi355 – 3617Combined sources
Helixi368 – 3703Combined sources
Helixi374 – 3763Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AMRX-ray1.25A29-383[»]
3AMSX-ray2.08A29-383[»]
ProteinModelPortaliO31097.
SMRiO31097. Positions 29-381.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO31097.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini30 – 362333BPPPROSITE-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.

O31097-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNHSKTLLLT AAAGLMLTCG AVSSQAKHKL SDPYHFTVNA AAETEPVDTA
60 70 80 90 100
GDAADDPAIW LDPKTPQNSK LITTNKKSGL VVYSLDGKML HSYNTGKLNN
110 120 130 140 150
VDIRYDFPLN GKKVDIAAAS NRSEGKNTIE IYAIDGKNGT LQSMTDPDHP
160 170 180 190 200
IATAINEVYG FTLYHSQKTG KYYAMVTGKE GEFEQYELKA DKNGYISGKK
210 220 230 240 250
VRAFKMNSQT EGMAADDEYG RLYIAEEDEA IWKFSAEPDG GSNGTVIDRA
260 270 280 290 300
DGRHLTRDIE GLTIYYAADG KGYLMASSQG NSSYAIYDRQ GKNKYVADFR
310 320 330 340 350
ITDGPETDGT SDTDGIDVLG FGLGPEYPFG IFVAQDGENI DHGQKANQNF
360 370 380
KIVPWERIAD QIGFRPLANE QVDPRKLTDR SGK
Length:383
Mass (Da):41,923
Last modified:January 1, 1998 - v1
Checksum:iE9BEC2E4A48EB9CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029053 Genomic DNA. Translation: AAC31775.1.
AJ277890 Genomic DNA. Translation: CAB91845.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF029053 Genomic DNA. Translation: AAC31775.1 .
AJ277890 Genomic DNA. Translation: CAB91845.1 .

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3AMR X-ray 1.25 A 29-383 [» ]
3AMS X-ray 2.08 A 29-383 [» ]
ProteinModelPortali O31097.
SMRi O31097. Positions 29-381.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Miscellaneous databases

EvolutionaryTracei O31097.

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. "Isolation, characterization, molecular gene cloning, and sequencing of a novel phytase from Bacillus subtilis."
    Kerovuo J., Lauraeus M., Nurminen P., Kalkkinen N., Apajalahti J.
    Appl. Environ. Microbiol. 64:2079-2085(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    Strain: VTT-E-68013.
  2. "Cloning of neutral phytase gene nphy from Bacillus subtilis and its expression in Escherichia coli."
    Yao B., Yuan T., Wang Y., Fan Y.
    Chin. J. Biotechnol. 17:11-15(2001)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: 981.

Entry informationi

Entry nameiPHYC_BACIU
AccessioniPrimary (citable) accession number: O31097
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: January 1, 1998
Last modified: November 26, 2014
This is version 72 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