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Protein
Submitted name:

Phospholipase D

Gene
N/A
Organism
Streptomyces sp. (strain PMF)
Status
Unreviewed-Annotation score: Annotation score: 1 out of 5-Experimental evidence at protein leveli

Functioni

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei167 – 1671NucleophileCombined sources
Sitei199 – 1991Important for catalytic activityCombined sources
Active sitei440 – 4401Proton donor/acceptorCombined sources
Sitei465 – 4651Important for catalytic activityCombined sources

GO - Molecular functioni

Complete GO annotation...

Enzyme and pathway databases

BRENDAi3.1.4.4. 1284.

Names & Taxonomyi

Protein namesi
Submitted name:
Phospholipase DImported (EC:3.1.4.4Imported)
OrganismiStreptomyces sp. (strain PMF)Imported
Taxonomic identifieri172564 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaStreptomycetalesStreptomycetaceaeStreptomyces

PTM / Processingi

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi52 ↔ 58Combined sources
Disulfide bondi224 ↔ 243Combined sources
Disulfide bondi295 ↔ 341Combined sources
Disulfide bondi415 ↔ 504Combined sources

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F0IX-ray1.40A4-504[»]
1V0RX-ray1.70A1-506[»]
1V0SX-ray1.75A1-506[»]
1V0TX-ray1.53A1-506[»]
1V0UX-ray1.42A1-506[»]
1V0VX-ray1.70A1-506[»]
1V0WX-ray1.35A1-506[»]
1V0YX-ray1.71A1-506[»]
ProteinModelPortaliP84147.
SMRiP84147. Positions 3-506.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP84147.

Family & Domainsi

Family and domain databases

InterProiIPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamiPF13091. PLDc_2. 1 hit.
[Graphical view]
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P84147-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
ADSATPHLDA VEQTLRQVSP GLEGDVWERT SGNKLDGSAA DPSDWLLQTP
60 70 80 90 100
GCWGDDKCAD RVGTKRLLAK MTENIGNATR TVDISTLAPF PNGAFQDAIV
110 120 130 140 150
AGLKESAAKG NKLKVRILVG AAPVYHMNVI PSKYRDELTA KLGKAAENIT
160 170 180 190 200
LNVASMTTSK TAFSWNHSKI LVVDGQSALT GGINSWKDDY LDTTHPVSDV
210 220 230 240 250
DLALTGPAAG SAGRYLDTLW TWTCQNKSNI ASVWFAASGN AGCMPTMHKD
260 270 280 290 300
TNPKASPATG NVPVIAVGGL GVGIKDVDPK STFRPDLPTA SDTKCVVGLH
310 320 330 340 350
DNTNADRDYD TVNPEESALR ALVASAKGHI EISQQDLNAT CPPLPRYDIR
360 370 380 390 400
LYDALAAKMA AGVKVRIVVS DPANRGAVGS GGYSQIKSLS EISDTLRNRL
410 420 430 440 450
ANITGGQQAA KTAMCSNLQL ATFRSSPNGK WADGHPYAQH HKLVSVDSST
460 470 480 490 500
FYIGSKNLYP SWLQDFGYIV ESPEAAKQLD AKLLDPQWKY SQETATVDYA

RGICNA
Length:506
Mass (Da):54,005
Last modified:September 13, 2004 - v1
Checksum:iC7420055940CBF27
GO

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1F0IX-ray1.40A4-504[»]
1V0RX-ray1.70A1-506[»]
1V0SX-ray1.75A1-506[»]
1V0TX-ray1.53A1-506[»]
1V0UX-ray1.42A1-506[»]
1V0VX-ray1.70A1-506[»]
1V0WX-ray1.35A1-506[»]
1V0YX-ray1.71A1-506[»]
ProteinModelPortaliP84147.
SMRiP84147. Positions 3-506.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.1.4.4. 1284.

Miscellaneous databases

EvolutionaryTraceiP84147.

Family and domain databases

InterProiIPR025202. PLD-like_dom.
IPR001736. PLipase_D/transphosphatidylase.
[Graphical view]
PfamiPF13091. PLDc_2. 1 hit.
[Graphical view]
SMARTiSM00155. PLDc. 2 hits.
[Graphical view]
PROSITEiPS50035. PLD. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The first crystal structure of a phospholipase D."
    Leiros I., Secundo F., Zambonelli C., Servi S., Hough E.
    Structure 8:655-667(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 4-504, DISULFIDE BONDS.
  2. "The reaction mechanism of phospholipase D from Streptomyces sp. strain PMF. Snapshots along the reaction pathway reveal a pentacoordinate reaction intermediate and an unexpected final product."
    Leiros I., McSweeney S., Hough E.
    J. Mol. Biol. 339:805-820(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS), ACTIVE SITE.

Entry informationi

Entry nameiP84147_STRSM
AccessioniPrimary (citable) accession number: P84147
Entry historyi
Integrated into UniProtKB/TrEMBL: September 13, 2004
Last sequence update: September 13, 2004
Last modified: June 24, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

3D-structureCombined sourcesImported

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.