TABLE 4.
Pairwise comparison of the structure of MmFadD32 with those of other adenylate-forming enzymes
| Protein name | Source | UniProtKB code | UniProtKB entry name | PDB code | Ref. | r.m.s.d./no. of aligned positions/sequence identity of aligned positions |
||
|---|---|---|---|---|---|---|---|---|
| N-terminal domain | C-terminal domain | Full length | ||||||
| FadD32 | M. marinum | B2HMK0 | FadD32_MYCMM | 5EY9 | This work | |||
| FadD32 | M. smegmatis | A0R618 | FadD32_MYCS2 | 5EY8 | This work | 1.0/466/74 | 0.6/128/79 | 1.1/595/75 |
| FadD28 | M. tuberculosis | P9WQ59 | FadD28_MYCTU | 3E53 | 41 | 1.7/417/38 | ||
| FadD13 | M. tuberculosis | P9WQ36 | FadD13_MYCTO | 3T5C | 43 | 2.4/377/20 | ||
| 3R44 | 42 | 2.7/380/20 | 2.0/99/22 | |||||
| FadD10 | M. tuberculosis | I6WXG2 | FadD10_MYCTU | 4IR7 | 44 | 2.7/362/18 | 2.3/104/20 | |
| Fatty acyl-AMP ligase | L. pneumophila | Q5ZTD3 | FAAL_LEGPH | 3KXW | 24 | 2.0/433/29 | 2.5 /102/24 | |
| Fatty acyl-AMP ligase | E. coli | Q8FDN4 | FAAL_ECOL6 | 3PBK | 24 | 2.4/421/30 | 1.8/103/33 | 2.5/524/ 30 |
| Benzoate-CoA ligase | B. xenovorans | Q13WK3 | BCL_BURXL | 2V7B | 45 | 2.5/375/18 | 1.8/94/19 | 2.8/469/19 |
| Malonyl-CoA synthetase MatB | R. palustris | Q6ND88 | MatB_RHOPA | 4FUT | 46 | 2.1/373/23 | 2.1/100/24 | 2.8/476/22 |
| Phenylalanine activating domain PheA of gramicidin S synthetase 1 | A. migulanus | P0C061 | GRSA_ANEMI | 1AMU | 47) | 2.4/382/19 | 2.2/97/14 | 3.1/481/18 |