B2HMK0
Gene name |
fadD32 (MMAR_5365) |
Protein name |
Long-chain-fatty-acid--AMP ligase FadD32 |
Names |
FAAL, Acyl-AMP synthetase |
Species |
Mycobacterium marinum (strain ATCC BAA-535 / M) |
KEGG Pathway |
mmi:MMAR_5365 |
EC number |
6.2.1.20: Acid--thiol ligases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
2 structures for B2HMK0
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 5EY9 | X-ray | 250 A | A/B | 1-629 | PDB |
| AF-B2HMK0-F1 | Predicted | AlphaFoldDB |
No variants for B2HMK0
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B2HMK0 | |||||
No associated diseases with B2HMK0
1 regional properties for B2HMK0
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | AMP-dependent synthetase/ligase domain | 26 - 489 | IPR000873 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.2.1.20 | Acid--thiol ligases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| long-chain fatty acid [acyl-carrier-protein] ligase activity | Catalysis of the reaction: ATP + an acid |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid metabolic process | +The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
| lipid biosynthetic process | The chemical reactions and pathways resulting in the formation of lipids, compounds soluble in an organic solvent but not, or sparingly, in an aqueous solvent. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAYHNPFIVN | GKIRFPENTN | LVRHVEKWAR | VRGDKLAYRF | LDFSTERDGV | ERDILWSEFS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ARNRAVGARL | QQVTQPGDRI | AILCPQNLDY | LISFFGALYS | GRIAVPLFDP | AEPGHVGRLH |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AVLDDCTPST | ILTTTDSAEG | VRKFIRSRSA | KERPRVIAVD | AVPTEVASTW | QQPEANELTT |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AYLQYTSGST | RVPSGVQITH | LNLPTNVLQV | LNALEGQEGD | RGVSWLPFFH | DMGLITVLLA |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SVLGHSFTFM | TPAAFVRRPG | RWIRELARKP | GETGGTFSAA | PNFAFEHAAM | RGVPRDDEPP |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LDLSNVKGIL | NGSEPVSPAS | MRKFFKAFEP | YGLRETAVKP | SYGLAEATLF | VSTTPMDEVP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TVIHVDRDEL | NKQRFVEVAA | DAPNAVAQVS | AGKVGVDEWA | VIVDTETASE | LPDGQIGEIW |
| 430 | 440 | 450 | 460 | 470 | 480 |
| LHGNNLGIGY | WGKEEESAQT | FRNILKSRVP | ESHAEGAPDD | GLWVRTGDYG | TYFKGHLYIA |
| 490 | 500 | 510 | 520 | 530 | 540 |
| GRIKDLVIID | GRNHYPQDLE | YTAQESTKAL | RVGYVAAFSV | PANQLPQKVF | DDPHAGLSFD |
| 550 | 560 | 570 | 580 | 590 | 600 |
| PEDTSEQLVI | VGERAAGTHK | LEYQPIADDI | RAAIAVGHGV | TVRDVLLVSA | GTIPRTSSGK |
| 610 | 620 | ||||
| IGRRACRTAY | IDGSLRSGVS | SPTVFATGS |