HMM Summary Page: TIGR00023

Functionacyl-phosphate glycerol 3-phosphate acyltransferase
Gene SymbolplsY
Trusted Cutoff137.20
Domain Trusted Cutoff137.20
Noise Cutoff62.40
Domain Noise Cutoff62.40
Isology Typeequivalog
EC Number2.3.1.-
HMM Length196
Mainrole CategoryFatty acid and phospholipid metabolism
Subrole CategoryBiosynthesis
Gene Ontology TermGO:0005886: plasma membrane cellular_component
GO:0006654: phosphatidic acid biosynthetic process biological_process
GO:0008374: O-acyltransferase activity molecular_function
AuthorHaft DH
Entry DateApr 20 1999 2:04PM
Last ModifiedFeb 14 2011 3:27PM
CommentThis HMM represents the full length of acylphosphate:glycerol 3-phosphate acyltransferase, and integral membrane protein about 200 amino acids in length, called PlsY in Streptococcus pneumoniae, YneS in Bacillus subtilis, and YgiH in E. coli. It is found in a single copy in a large number of bacteria, including the Mycoplasmas but not Mycobacteria or spirochetes, for example. Its partner is PlsX (see TIGR00182), and the pair can replace PlsB for synthesizing 1-acylglycerol-3-phosphate.
ReferencesRN [1] RM PMID:17308305 RT Topology and active site of PlsY: the bacterial acylphosphate:glycerol-3-phosphate acyltransferase. RA Lu YJ, Zhang F, Grimes KD, Lee RE, Rock CO RL J Biol Chem. 2007 Apr 13;282(15):11339-46. Epub 2007 Feb 16. RN [2] RM PMID:17645809 RT Involvement of the YneS/YgiH and PlsX proteins in phospholipid biosynthesis in both Bacillus subtilis and Escherichia coli. RA Yoshimura M, Oshima T, Ogasawara N RL BMC Microbiol. 2007 Jul 24;7:69. DR InterPro; IPR003811; DUF205 DR PFAM; PF02660; DUF205 SE TIGR AL clustalw DR HAMAP; MF_01043; 351 of 377
Genome PropertyGenProp0837: 1-acylglycerol-3-phosphate biosynthesis, PlsX/Y pathway (HMM)