Skip Header

Contribute Send feedback
Read comments (?) or add your own

C5B706 (PLSB_EDWI9) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 17. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Glycerol-3-phosphate acyltransferase

Short name=GPAT
EC=2.3.1.15
Gene names
Name:plsB
Ordered Locus Names:NT01EI_0225
OrganismEdwardsiella ictaluri (strain 93-146) [Complete proteome] [HAMAP]
Taxonomic identifier634503 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEdwardsiella

Protein attributes

Sequence length818 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

Acyl-CoA + sn-glycerol 3-phosphate = CoA + 1-acyl-sn-glycerol 3-phosphate. HAMAP MF_00393

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 1/3. HAMAP MF_00393

Subcellular location

Cell inner membrane; Peripheral membrane protein; Cytoplasmic side By similarity HAMAP MF_00393.

Domain

The HXXXXD motif is essential for acyltransferase activity and may constitute the binding site for the phosphate moiety of the glycerol-3-phosphate By similarity. HAMAP MF_00393

Sequence similarities

Belongs to the GPAT/DAPAT family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   Molecular functionAcyltransferase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processphospholipid biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionglycerol-3-phosphate O-acyltransferase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 818818Glycerol-3-phosphate acyltransferase HAMAP MF_00393
PRO_1000205849

Regions

Motif305 – 3106HXXXXD motif HAMAP MF_00393

Sequences

Sequence LengthMass (Da)Tools
C5B706 [UniParc].

Last modified July 28, 2009. Version 1.
Checksum: C22D7ADC3D55C290

FASTA81892,827
        10         20         30         40         50         60 
MSGWRKIYYK LLNLILKLLV KSKVIPTDPV AELRLDTTRP VFYVLPYNSK VDLLTLRDRC 

        70         80         90        100        110        120 
LALDLPDPLD DNEIDGVILP RYVFIDDGPR VFRYYAPKQA SVKLFLDYLD LHRGNPSLDI 

       130        140        150        160        170        180 
QMIPVSVMFG RAPGREDHKG APQLRLLNGI QKFFAVLWLG RDSFVRFSNT VSLRYMADEH 

       190        200        210        220        230        240 
GTDKTIAQKL ARVARMHFSR LRLAAVGPRL PDRQALFNKL LGSKAIEKAV EDEARSKKIS 

       250        260        270        280        290        300 
REKAQQNAVA LMEEIAADFT YEAVRLSDRV LSWTWNRLYQ GINVHNAERV RQLAQDGHEI 

       310        320        330        340        350        360 
VYVPCHRSHM DYLLLSYVLY HQGLVPPHIA AGINLNFWPA GPIFRRLGAF FIRRTFKGNK 

       370        380        390        400        410        420 
LYSTVFREYL GELFSRGYSV EYFMEGGRSR TGRLLEPKTG TLAMTLQAML RGGKRPITLV 

       430        440        450        460        470        480 
PVYIGYEHVM EVATYAKELR GATKEKESLP QMVRGLRKLR NLGQGYVNFG EPISLNVWLN 

       490        500        510        520        530        540 
QHVPEWREAI DPIEAQRPHW LPASVNSIAG EVMVNINKAA AANAMNLCAT ALLASRQRAL 

       550        560        570        580        590        600 
TREQLLEQLE CYLQLLQNVP YAPDATLPQR TPQELLDHAL QMNKFEVEKD NIGDLIILPR 

       610        620        630        640        650        660 
EQAVLMTYYR NNIQHMLVLP ALVASMVIHH RQISRDELLR QAAVIYPMLK QELFMHYVPE 

       670        680        690        700        710        720 
TLPQVLSPII DELCRQQLIS LQDDTLIINP PRIRSLQLLA AGVRETLQRY AITFSLLSAN 

       730        740        750        760        770        780 
PSISRGALEK ESRILAQRLS LLHGINAPEF FDKAVFATLV ATLRAEGYIN DVGDAVREQT 

       790        800        810 
LEIYNLLADL LTPEIRLTIE SVSIAALEDT GGADGGTA 

« Hide

References

[1]"Complete genome sequence of Edwardsiella ictaluri 93-146."
Williams M.L., Gillaspy A.F., Dyer D.W., Thune R.L., Waldbieser G.C., Schuster S.C., Gipson J., Zaitshik J., Landry C., Lawrence M.L.
Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 93-146.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001600 Genomic DNA. Translation: ACR67468.1.
RefSeqYP_002931703.1. NC_012779.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC5B706.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7960249.
GenomeReviewsGene locus NT01EI_0225 in contig CP001600_GR.
KEGGeic:NT01EI_0225.
PATRIC21833728. VBIEdwIct114273_0201.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAWNKLYQG.
ProtClustDBPRK04974.

Family and domain databases

HAMAPMF_00393. Glyc3P_acyltrans.
[Tree]
InterProIPR002123. Acyltransferase.
IPR022284. G3P_O-AcylTrfase.
[Graphical view]
KOK00631.
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
PIRSFPIRSF000437. GPAT_DHAPAT. 1 hit.
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR03703. PlsB. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLSB_EDWI9
AccessionPrimary (citable) accession number: C5B706
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: July 28, 2009
Last modified: January 25, 2012
This is version 17 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families