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Protein

1-phosphatidylinositol phosphodiesterase

Gene
N/A
Organism
Bacillus cereus
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Cleaves glycosylphosphatidylinositol (GPI) and phosphatidylinositol (PI) anchors but not PI phosphates.

Catalytic activityi

1-phosphatidyl-1D-myo-inositol = 1D-myo-inositol 1,2-cyclic phosphate + 1,2-diacyl-sn-glycerol.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei63 – 631Proton acceptor
Active sitei113 – 1131Proton donor

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15192.

Names & Taxonomyi

Protein namesi
Recommended name:
1-phosphatidylinositol phosphodiesterase (EC:4.6.1.13)
Alternative name(s):
Phosphatidylinositol diacylglycerol-lyase
Phosphatidylinositol-specific phospholipase C
Short name:
PI-PLC
OrganismiBacillus cereus
Taxonomic identifieri1396 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 3131Add
BLAST
Chaini32 – 3292981-phosphatidylinositol phosphodiesterasePRO_0000024294Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi226900.BC3761.

Structurei

Secondary structure

1
329
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi35 – 395Combined sources
Helixi41 – 433Combined sources
Turni44 – 474Combined sources
Turni54 – 563Combined sources
Beta strandi59 – 624Combined sources
Helixi65 – 673Combined sources
Helixi73 – 797Combined sources
Helixi86 – 905Combined sources
Turni91 – 933Combined sources
Beta strandi96 – 1038Combined sources
Beta strandi109 – 1135Combined sources
Beta strandi116 – 1216Combined sources
Helixi122 – 13514Combined sources
Beta strandi141 – 1477Combined sources
Helixi159 – 1668Combined sources
Turni167 – 1693Combined sources
Beta strandi170 – 1734Combined sources
Helixi182 – 1854Combined sources
Beta strandi188 – 1947Combined sources
Beta strandi211 – 2188Combined sources
Beta strandi220 – 2223Combined sources
Beta strandi224 – 2285Combined sources
Helixi235 – 25016Combined sources
Turni251 – 2544Combined sources
Beta strandi258 – 2636Combined sources
Beta strandi271 – 2755Combined sources
Helixi276 – 29419Combined sources
Beta strandi301 – 3055Combined sources
Beta strandi311 – 3133Combined sources
Helixi315 – 3217Combined sources
Helixi322 – 3265Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYMX-ray2.20A32-329[»]
1PTDX-ray2.60A32-329[»]
1PTGX-ray2.60A32-329[»]
2PTDX-ray2.00A32-329[»]
3PTDX-ray2.20A32-329[»]
4PTDX-ray2.30A32-329[»]
5PTDX-ray2.70A32-329[»]
6PTDX-ray2.60A32-329[»]
7PTDX-ray2.60A32-329[»]
ProteinModelPortaliP14262.
SMRiP14262. Positions 32-327.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP14262.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini53 – 194142PI-PLC X-boxPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 PI-PLC X-box domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF00388. PI-PLC-X. 1 hit.
[Graphical view]
SMARTiSM00148. PLCXc. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS50007. PIPLC_X_DOMAIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P14262-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD
60 70 80 90 100
SIPLARISIP GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR
110 120 130 140 150
GRLTDDNTIV LHHGPLYLYV TLHEFINEAK QFLKDNPSET IIMSLKKEYE
160 170 180 190 200
DMKGAEDSFS STFEKKYFVD PIFLKTEGNI KLGDARGKIV LLKRYSGSNE
210 220 230 240 250
PGGYNNFYWP DNETFTTTVN QNANVTVQDK YKVSYDEKVK SIKDTMDETM
260 270 280 290 300
NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIANY IKQKNPARVG
310 320
WVIQDYINEK WSPLLYQEVI RANKSLIKE
Length:329
Mass (Da):38,109
Last modified:January 1, 1990 - v1
Checksum:i0D731F5604135CB4
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30809 Genomic DNA. Translation: AAA22665.1.
PIRiA33493.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M30809 Genomic DNA. Translation: AAA22665.1.
PIRiA33493.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1GYMX-ray2.20A32-329[»]
1PTDX-ray2.60A32-329[»]
1PTGX-ray2.60A32-329[»]
2PTDX-ray2.00A32-329[»]
3PTDX-ray2.20A32-329[»]
4PTDX-ray2.30A32-329[»]
5PTDX-ray2.70A32-329[»]
6PTDX-ray2.60A32-329[»]
7PTDX-ray2.60A32-329[»]
ProteinModelPortaliP14262.
SMRiP14262. Positions 32-327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi226900.BC3761.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-15192.

Miscellaneous databases

EvolutionaryTraceiP14262.

Family and domain databases

Gene3Di3.20.20.190. 1 hit.
InterProiIPR017946. PLC-like_Pdiesterase_TIM-brl.
IPR000909. PLipase_C_PInositol-sp_X_dom.
[Graphical view]
PfamiPF00388. PI-PLC-X. 1 hit.
[Graphical view]
SMARTiSM00148. PLCXc. 1 hit.
[Graphical view]
SUPFAMiSSF51695. SSF51695. 1 hit.
PROSITEiPS50007. PIPLC_X_DOMAIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Phosphatidylinositol-specific phospholipase C of Bacillus cereus: cloning, sequencing, and relationship to other phospholipases."
    Kuppe A., Evans L.M., McMillen D.A., Griffith O.H.
    J. Bacteriol. 171:6077-6083(1989) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol."
    Heinz D.W., Ryan M., Bullock T.L., Griffith O.H.
    EMBO J. 14:3855-3863(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS).
  3. "Crystal structure of phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with glucosaminyl(alpha 1-->6)-D-myo-inositol, an essential fragment of GPI anchors."
    Heinz D.W., Ryan M., Smith M.P., Weaver L.H., Keana J.F., Griffith O.H.
    Biochemistry 35:9496-9504(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
  4. "Probing the roles of active site residues in phosphatidylinositol-specific phospholipase C from Bacillus cereus by site-directed mutagenesis."
    Gassler C.S., Ryan M., Liu T., Griffith O.H., Heinz D.W.
    Biochemistry 36:12802-12813(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).

Entry informationi

Entry nameiPLC_BACCE
AccessioniPrimary (citable) accession number: P14262
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 1, 1990
Last modified: June 24, 2015
This is version 88 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

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

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 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.