Accession | TIGR01734 |
Name | D-ala-DACP-lig |
Function | D-alanine--poly(phosphoribitol) ligase, subunit 1 |
Gene Symbol | dltA |
Trusted Cutoff | 559.85 |
Domain Trusted Cutoff | 559.85 |
Noise Cutoff | 487.60 |
Domain Noise Cutoff | 487.60 |
Isology Type | equivalog |
EC Number | 6.1.1.13 |
HMM Length | 504 |
Mainrole Category | Cell envelope |
Subrole Category | Biosynthesis and degradation of murein sacculus and peptidoglycan |
Gene Ontology Term | GO:0019350: teichoic acid biosynthetic process biological_process |
| GO:0047473: D-alanine-poly(phosphoribitol) ligase activity molecular_function |
Author | Selengut J |
Entry Date | Nov 1 2002 4:58PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides [1]. |
References | RN [1]
RM PMID: 7797557
RT Incorporation of D-alanine into lipoteichoic acid and wall teichoic acid in Bacillus subtilis. Identification of genes and regulation.
RA Perego M, Glaser P, Minutello A, Strauch MA, Leopold K, Fischer W.
RL J Biol Chem 1995 Jun 30;270(26):15598-606
DR HAMAP; MF_00593; 53 of 53 |
Genome Property | GenProp0958: D-alanyl-lipoteichoic acid biosynthesis (HMM) |