Accession | TIGR01205 |
Name | D_ala_D_alaTIGR |
Function | D-alanine--D-alanine ligase |
Trusted Cutoff | 245.65 |
Domain Trusted Cutoff | 245.65 |
Noise Cutoff | 95.55 |
Domain Noise Cutoff | 95.55 |
Isology Type | subfamily |
EC Number | 6.3.2.4 |
HMM Length | 318 |
Mainrole Category | Cell envelope |
Subrole Category | Biosynthesis and degradation of murein sacculus and peptidoglycan |
Gene Ontology Term | GO:0008716: D-alanine-D-alanine ligase activity molecular_function |
| GO:0009252: peptidoglycan biosynthetic process biological_process |
Author | Haft DH |
Entry Date | Mar 20 2001 10:30AM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This model describes D-Ala--D-Ala ligase, an enzyme that makes a required precursor of the bacterial cell wall. It also describes some closely related proteins responsible for resistance to glycopeptide antibiotics such as vancomycin. The mechanism of glyopeptide antibiotic resistance involves the production of D-alanine-D-lactate (VanA and VanB families) or D-alanine-D-serine (VanC). The seed alignment contains only chromosomally encoded D-ala--D-ala ligases,
but a number of antibiotic resistance proteins score above the trusted cutoff of this model. |
References | Changes in small numbers of amino acids, as demonstrated crystallographically, can alter specificity.
DR HAMAP; MF_00047; 436 of 456 |
Genome Property | GenProp0158: peptidoglycan(murein) biosynthesis (HMM) |