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Q59601 (PLSC_NEIGO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 31, 2011. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
1-acyl-sn-glycerol-3-phosphate acyltransferase

Short name=1-AGP acyltransferase
Short name=1-AGPAT
EC=2.3.1.51
Alternative name(s):
Lysophosphatidic acid acyltransferase
Short name=LPAAT
Gene names
Name:plsC
OrganismNeisseria gonorrhoeae
Taxonomic identifier485 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length255 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Converts lysophosphatidic acid (LPA) into phosphatidic acid by incorporating acyl moiety at the 2 position.

Catalytic activity

Acyl-CoA + 1-acyl-sn-glycerol 3-phosphate = CoA + 1,2-diacyl-sn-glycerol 3-phosphate.

Pathway

Phospholipid metabolism; CDP-diacylglycerol biosynthesis; CDP-diacylglycerol from sn-glycerol 3-phosphate: step 2/3.

Subcellular location

Cell inner membrane; Peripheral membrane protein.

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.

Sequence similarities

Belongs to the 1-acyl-sn-glycerol-3-phosphate acyltransferase family.

Ontologies

Keywords
   Biological processPhospholipid biosynthesis
   Cellular componentCell inner membrane
Cell membrane
Membrane
   Molecular functionAcyltransferase
Transferase
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 function1-acylglycerol-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 – 2552551-acyl-sn-glycerol-3-phosphate acyltransferase
PRO_0000208174

Regions

Motif78 – 836HXXXXD motif

Sequences

Sequence LengthMass (Da)Tools
Q59601 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 833F080361A5CE88

FASTA25527,830
        10         20         30         40         50         60 
MSSNKASFFT RLRRLCRLTV WLFKTGKNLR GIDGGCPKSR NRAVIALGKG ALAALDIGLE 

        70         80         90        100        110        120 
VGRPAPEHPN GVLVAANHVS WLDIFAMSAV YPSSFIAKQE IKSWPVLGKM GQNAGTVFIN 

       130        140        150        160        170        180 
RNSRRDIEPI NRAVCETLQR GQNVSFFPEA RTSSGLGLLP FKAALFQSAI DAGAKVLAVA 

       190        200        210        220        230        240 
LRYYDETGKR TARPSYADVG LPTCLWRIVS MKKLTIKVDF VCVADAAESE DRYALKDKIE 

       250 
ESIRAVVADD ADIAV 

« Hide

References

[1]"Membrane glycerophospholipid biosynthesis in Neisseria meningitidis and Neisseria gonorrhoeae: identification, characterization, and mutagenesis of a lysophosphatidic acid acyltransferase."
Swartley J.S., Balthazar J.T., Coleman J., Shafer W.M., Stephens D.S.
Mol. Microbiol. 18:401-412(1995) [PubMed: 8748025] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: FA19.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U21806 Genomic DNA. Translation: AAB40877.1.
PIRS70545.

3D structure databases

ProteinModelPortalQ59601.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.3.1.51. 3590.

Family and domain databases

InterProIPR002123. Acyltransferase.
IPR004552. AGP_acyltrans.
[Graphical view]
PfamPF01553. Acyltransferase. 1 hit.
[Graphical view]
SMARTSM00563. PlsC. 1 hit.
[Graphical view]
TIGRFAMsTIGR00530. AGP_acyltrn. 1 hit.
ProtoNetSearch...

Entry information

Entry namePLSC_NEIGO
AccessionPrimary (citable) accession number: Q59601
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: November 1, 1996
Last modified: May 31, 2011
This is version 50 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