AMP-binding, conserved site
Short name | AMP-binding_CS |
Description
* Insects luciferase (luciferin 4-monooxygenase) (
* Alpha-aminoadipate reductase (
* Acetate--CoA ligase (
* Long-chain-fatty-acid--CoA ligase (
* 4-coumarate--CoA ligase (
* O-succinylbenzoic acid--CoA ligase (
* 4-Chlorobenzoate--CoA ligase (
* Indoleacetate--lysine ligase (
* Bile acid-CoA ligase (gene baiB) from Eubacterium sp. (strain VPI 12708)
* Crotonobetaine/carnitine-CoA ligase (
* L-(alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase (ACV synthetase) from various fungi (gene acvA or pcbAB). This enzyme catalyzes the first step in the biosynthesis of penicillin and cephalosporin, the formation of ACV from the constituent amino acids. The amino acids seem to be activated by adenylation. It is a protein of around 3700 amino acids that contains three related domains of about 1000 amino acids.
* Gramicidin S synthetase I (gene grsA) from Brevibacillus brevis (Bacillus brevis). This enzyme catalyses the first step in the biosynthesis of the cyclic antibiotic gramicidin S, the ATP-dependent racemization of phenylalanine (
* Tyrocidine synthetase I (gene tycA) from B. brevis. The reaction carried out by tycA is identical to that catalysed by GrsA
* Gramicidin S synthetase II (gene grsB) from B. brevis. This enzyme is a multifunctional protein that activates and polymerises proline, valine, ornithine and leucine. GrsB consists of four related domains.
* Enterobactin synthetase components E (gene entE) and F (gene entF) from E. coli. These two enzymes are involved in the ATP-dependent activation of respectively 2,3-dihydroxybenzoate and serine during enterobactin (enterochelin) biosynthesis.
* Cyclic peptide antibiotic surfactin synthase subunits 1, 2 and 3 from Bacillus subtilis. Subunits 1 and 2 contains three related domains while subunit 3 only contains a single domain.
* HC-toxin synthetase (gene HTS1) from Cochliobolus carbonum (Bipolaris zeicola). This enzyme activates the four amino acids (Pro, L-Ala, D-Ala and 2-amino-9,10-epoxi-8-oxodecanoic acid) that make up HC-toxin, a cyclic tetrapeptide. HTS1 consists of four related domains.
* ORA (octapeptide-repeat antigen), a Plasmodium falciparum protein whose function is not known but which shows a high degree of similarity with the above proteins.
* AngR, a Vibrio anguillarum (Listonella anguillarum) protein. AngR is thought to be a transcriptional activator which modulates the anguibactin (an iron-binding siderophore) biosynthesis gene cluster operon. But we believe, that AngR is not a DNA-binding protein, but rather an enzyme involved in the biosynthesis of anguibactin. This conclusion is based on three facts: the presence of the AMP-binding domain; the size of AngR (1048 residues), which is far bigger than any bacterial transcriptional protein; and the presence of a probable S-acyl thioesterase immediately downstream of the gene for AngR.
* A hypothetical protein in MmsB 3'region in Pseudomonas aeruginosa.
* E. coli hypothetical protein YdiD.
* Yeast hypothetical protein YBR041w.
* Yeast hypothetical protein YBR222c.
* Yeast hypothetical protein YER147c.
References
1.Sequence analysis of firefly luciferase family reveals a conservative sequence motif. Toh H. Protein Seq. Data Anal. 4, 111-7, (1991). PMID: 1946328
2.The multifunctional peptide synthetase performing the first step of penicillin biosynthesis in Penicillium chrysogenum is a 421,073 dalton protein similar to Bacillus brevis peptide antibiotic synthetases. Smith DJ, Earl AJ, Turner G. EMBO J. 9, 2743-50, (1990). View articlePMID: 2118102
3.The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase. Mallonee DH, Adams JL, Hylemon PB. J. Bacteriol. 174, 2065-71, (1992). View articlePMID: 1551828
4.Four homologous domains in the primary structure of GrsB are related to domains in a superfamily of adenylate-forming enzymes. Turgay K, Krause M, Marahiel MA. Mol. Microbiol. 6, 529-46, (1992). View articlePMID: 1560782
5.Sequence organization and regulation of the Bacillus subtilis menBE operon. Driscoll JR, Taber HW. J. Bacteriol. 174, 5063-71, (1992). View articlePMID: 1629163
6.Ancestry of the 4-chlorobenzoate dehalogenase: analysis of amino acid sequence identities among families of acyl:adenyl ligases, enoyl-CoA hydratases/isomerases, and acyl-CoA thioesterases. Babbitt PC, Kenyon GL, Martin BM, Charest H, Slyvestre M, Scholten JD, Chang KH, Liang PH, Dunaway-Mariano D. Biochemistry 31, 5594-604, (1992). View articlePMID: 1351742
7.A regulatory gene, angR, of the iron uptake system of Vibrio anguillarum: similarity with phage P22 cro and regulation by iron. Farrell DH, Mikesell P, Actis LA, Crosa JH. Gene 86, 45-51, (1990). View articlePMID: 2311935
Cross References
ENZYME
- 1.1.1.-
- 1.13.12.7
- 1.2.1.-
- 1.2.1.101
- 1.2.1.30
- 1.2.1.31
- 1.2.1.95
- 2.1.1.-
- 2.3.1.-
- 2.3.1.40
- 2.3.2.-
- 2.7.7.97
- 2.8.1.9
- 3.3.2.-
- 5.1.1.-
- 5.1.1.11
- 5.1.1.12
- 5.1.1.13
- 5.1.1.3
- 6.1.2.-
- 6.1.3.1
- 6.2.1.-
- 6.2.1.1
- 6.2.1.12
- 6.2.1.13
- 6.2.1.15
- 6.2.1.16
- 6.2.1.17
- 6.2.1.2
- 6.2.1.20
- 6.2.1.24
- 6.2.1.25
- 6.2.1.26
- 6.2.1.27
- 6.2.1.3
- 6.2.1.32
- 6.2.1.33
- 6.2.1.34
- 6.2.1.36
- 6.2.1.40
- 6.2.1.41
- 6.2.1.42
- 6.2.1.43
- 6.2.1.44
- 6.2.1.46
- 6.2.1.47
- 6.2.1.48
- 6.2.1.53
- 6.2.1.54
- 6.2.1.60
- 6.2.1.61
- 6.2.1.62
- 6.2.1.63
- 6.2.1.65
- 6.2.1.66
- 6.2.1.67
- 6.2.1.68
- 6.2.1.69
- 6.2.1.7
- 6.2.1.70
- 6.2.1.71
- 6.2.1.72
- 6.2.1.75
- 6.2.1.76
- 6.2.1.8
- 6.3.1.-
- 6.3.1.15
- 6.3.2.-
- 6.3.2.14
- 6.3.2.20
- 6.3.2.26
- 6.3.2.40
- 6.3.2.50
- 6.3.3.-
- 6.7.1.1
- 6.7.1.2
Contributing Member Database Entry
- PROSITE patterns:PS00455