| Accession | TIGR00182 |
| Name | plsX |
| Function | fatty acid/phospholipid synthesis protein PlsX |
| Gene Symbol | plsX |
| Trusted Cutoff | 243.40 |
| Domain Trusted Cutoff | 243.40 |
| Noise Cutoff | 177.85 |
| Domain Noise Cutoff | 177.85 |
| Isology Type | equivalog |
| HMM Length | 337 |
| Mainrole Category | Fatty acid and phospholipid metabolism |
| Subrole Category | Biosynthesis |
| Gene Ontology Term | GO:0003824: catalytic activity molecular_function |
| | GO:0008610: lipid biosynthetic process biological_process |
| Author | Richardson DL |
| Entry Date | Apr 20 1999 2:09PM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | This protein of fatty acid/phospholipid biosynthesis, called PlsX after the member in Streptococcus pneumoniae, is proposed to be a phosphate acyltransferase that partners with PlsY (TIGR00023) in a two-step 1-acylglycerol-3-phosphate biosynthesis pathway alternative to the one-step PlsB (EC 2.3.1.15) pathway. |
| References | RN [1]
RM PMID:19058030
RT Crystal structure of fatty acid/phospholipid synthesis protein PlsX from Enterococcus faecalis.
RA Kim Y, Li H, Binkowski TA, Holzle D, Joachimiak A
RL J Struct Funct Genomics. 2008 Dec 5.
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 PFAM; PF02504
DR InterPro; IPR003664
DR ECOCYC; EG11437; plsX
SE TIGR
DR HAMAP; MF_00019; 411 of 415 |
| Genome Property | GenProp0837: 1-acylglycerol-3-phosphate biosynthesis, PlsX/Y pathway (HMM) |
