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Protein

1-phosphatidylinositol phosphodiesterase

Gene
N/A
Organism
Bacillus thuringiensis
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)DescriptionActionsGraphical viewLength
Active sitei63Proton acceptorPROSITE-ProRule annotation1
Active sitei113Proton donorPROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Lyase

Keywords - Biological processi

Lipid degradation, Lipid metabolism

Enzyme and pathway databases

BRENDAi4.6.1.13. 711.
SABIO-RKP08954.

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 thuringiensis
Taxonomic identifieri1428 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillusBacillus cereus group

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 31Add BLAST31
ChainiPRO_000002429532 – 3291-phosphatidylinositol phosphodiesteraseAdd BLAST298

Structurei

Secondary structure

1329
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi35 – 39Combined sources5
Beta strandi41 – 43Combined sources3
Turni44 – 47Combined sources4
Turni54 – 56Combined sources3
Beta strandi59 – 62Combined sources4
Turni63 – 66Combined sources4
Helixi68 – 71Combined sources4
Helixi73 – 79Combined sources7
Helixi86 – 91Combined sources6
Beta strandi96 – 103Combined sources8
Beta strandi109 – 113Combined sources5
Beta strandi116 – 121Combined sources6
Helixi122 – 135Combined sources14
Beta strandi141 – 147Combined sources7
Helixi159 – 166Combined sources8
Turni167 – 169Combined sources3
Helixi182 – 185Combined sources4
Beta strandi188 – 196Combined sources9
Beta strandi213 – 218Combined sources6
Beta strandi220 – 222Combined sources3
Beta strandi224 – 228Combined sources5
Helixi235 – 250Combined sources16
Turni251 – 254Combined sources4
Beta strandi258 – 263Combined sources6
Helixi272 – 274Combined sources3
Helixi276 – 294Combined sources19
Beta strandi301 – 305Combined sources5
Beta strandi308 – 313Combined sources6
Helixi315 – 321Combined sources7
Helixi322 – 326Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T6MX-ray2.11A/B32-329[»]
2OR2X-ray1.84A/B32-327[»]
3EA1X-ray1.75A/B32-329[»]
3EA2X-ray1.95A/B32-329[»]
3EA3X-ray1.78A/B32-329[»]
ProteinModelPortaliP08954.
SMRiP08954.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP08954.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini51 – 194PI-PLC X-boxPROSITE-ProRule annotationAdd BLAST144

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.

P08954-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKKLILKL FICSTIFITF VFALHDKRVV AASSVNELEN WSKWMQPIPD
60 70 80 90 100
NIPLARISIP GTHDSGTFKL QNPIKQVWGM TQEYDFRYQM DHGARIFDIR
110 120 130 140 150
GRLTDDNTIV LHHGPLYLYV TLHEFINEAK QFLKDNPSET IIMSLKKEYE
160 170 180 190 200
DMKGAEGSFS STFEKNYFVD PIFLKTEGNI KLGDARGKIV LLKRYSGSNE
210 220 230 240 250
SGGYNNFYWP DNETFTTTVN QNVNVTVQDK YKVNYDEKVK SIKDTMDETM
260 270 280 290 300
NNSEDLNHLY INFTSLSSGG TAWNSPYYYA SYINPEIAND IKQKNPTRVG
310 320
WVIQDYINEK WSPLLYQEVI RANKSLIKE
Length:329
Mass (Da):38,091
Last modified:November 1, 1988 - v1
Checksum:iCB89586F3195267C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12952 Genomic DNA. Translation: CAA31410.1.
X14178 Genomic DNA. Translation: CAA32378.1.
PIRiA30760.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X12952 Genomic DNA. Translation: CAA31410.1.
X14178 Genomic DNA. Translation: CAA32378.1.
PIRiA30760.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1T6MX-ray2.11A/B32-329[»]
2OR2X-ray1.84A/B32-327[»]
3EA1X-ray1.75A/B32-329[»]
3EA2X-ray1.95A/B32-329[»]
3EA3X-ray1.78A/B32-329[»]
ProteinModelPortaliP08954.
SMRiP08954.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi4.6.1.13. 711.
SABIO-RKP08954.

Miscellaneous databases

EvolutionaryTraceiP08954.

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...

Entry informationi

Entry nameiPLC_BACTU
AccessioniPrimary (citable) accession number: P08954
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: November 1, 1988
Last modified: November 2, 2016
This is version 97 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

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 one 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.