Top Level Name
⌊ Superfamily (core) Radical SAM
⌊ Subgroup PLP-dependent
⌊ Family arginine 2,3-aminomutase
| Total |
100%  |
<100% |
|||
| Functional domains | 26 | 26 | 0 | ||
| UniProtKB | 43 | 43 | 0 | ||
| GI | 67 | 67 | 0 | ||
| Structures | 0 | ||||
| Reactions | 1 | ||||
| Functional domains of this family were last updated on June 10, 2017 | |||||
| New functional domains were last added to this family on June 22, 2014 | |||||
Similarity to Lysine 2,3-aminomutase and Glutamate 2,3-aminomutase suggests membership of this sub-group. Different residues at the probable amino acid binding site suggest a different substrate specificity, probably arginine. Very little appears to be known about this family of enzymes.
Cone MC, Yin X, Grochowski LL, Parker MR, Zabriskie TM
The blasticidin S biosynthesis gene cluster from Streptomyces griseochromogenes: sequence analysis, organization, and initial characterization
▸ Abstract
Chembiochem 828;2003(4):9-821 | PubMed ID: 12964155
Lysine and Cysteine residues identified on strength of alignment. Although Thr324 and Asp287 (in EFD 386083) appear to match up with the Glu and Lys binding residues in the other KamA proteins, these are not 100% conserved in the alignment. Thus, they have not been annotated in the conserved alignment residues.
Static File Downloads
| File Name | Description | Parameters | Stats |
|---|---|---|---|
| network.fam291.bs60.mek250K.xgmml | One node per sequence network | min bit score = 60 max edge count = 250K |
size = 204K num_edges = 325 num_nodes = 26 |
| sfld_alignment_fam291.msa | Annotated Sequence Alignment, Stockholm format | 9 sequences size: 5.4K |
