B5VLD2
Gene name |
AIM22 (AWRI1631_101610) |
Protein name |
Putative lipoate-protein ligase A |
Names |
Altered inheritance rate of mitochondria protein 22 |
Species |
Saccharomyces cerevisiae (strain AWRI1631) (Baker's yeast) |
KEGG Pathway |
|
EC number |
6.3.1.20: Acid--ammonia (or amine) ligases (amide synthases) |
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
1 structures for B5VLD2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-B5VLD2-F1 | Predicted | AlphaFoldDB |
No variants for B5VLD2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for B5VLD2 | |||||
No associated diseases with B5VLD2
7 regional properties for B5VLD2
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Translational (tr)-type GTP-binding domain | 10 - 201 | IPR000795 |
| domain | Translation elongation factor EFTu/EF1A, C-terminal | 295 - 389 | IPR004160 |
| domain | Translation elongation factor EFTu-like, domain 2 | 222 - 291 | IPR004161 |
| domain | Small GTP-binding protein domain | 13 - 143 | IPR005225 |
| conserved_site | Tr-type G domain, conserved site | 46 - 61 | IPR031157 |
| domain | Elongation factor Tu, domain 2 | 208 - 294 | IPR033720 |
| domain | Elongation factor Tu (EF-Tu), GTP-binding domain | 11 - 200 | IPR041709 |
Functions
| Description | ||
|---|---|---|
| EC Number | 6.3.1.20 | Acid--ammonia (or amine) ligases (amide synthases) |
| 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. |
| lipoate-protein ligase activity | Catalysis of the lipoylation of a protein in two steps: ATP + (R)-lipoate + a -N6-(lipoyl)lysine + AMP + diphosphate (overall reaction): (1) ATP + (R)-lipoate = lipoyl-AMP + diphosphate; (2) lipoyl-AMP + a -N6-(lipoyl)lysine + AMP. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| protein lipoylation | The lipoylation of peptidyl-lysine to form peptidyl-N6-lipoyl-L-lysine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSMMLSNWAL | SPRYVGQRNL | IHCTTLFHTL | TRWAKDADDK | YHDINSMYEN | MFTPSNDNVS |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ILQDEGKSDY | DTTKTSSMQE | DISAFNKDLY | NFYNIGYAKQ | IMSASQLENI | VKAKGRFVIQ |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SLSTSPYYNL | ALENYVFKNT | PRAKRGPDNC | RLLFYINDRC | AVIGKNQNLW | QEVDLAKLKS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KNFELLRRFS | GGGTVLHDLG | NVNYSYLTSR | EKFETKFFNK | MIIKWLNSLN | PELRLDLNER |
| 250 | 260 | 270 | 280 | 290 | 300 |
| GDIIQDGFKI | SGSAYKIAGG | KAYHHATMLL | NADLEQFSGL | LEPSLPNNME | WESSGVHSVK |
| 310 | 320 | 330 | 340 | 350 | 360 |
| SKIKNVGIIT | PNQFIAVVSE | RFQKTFKVDG | EIPIYYCDEF | KSINDEIKDA | MNTLQSEQWK |
| 370 | 380 | 390 | 400 | ||
| YFSGPKFSVK | IKDKGLTIKV | EKGMIYDCDR | NDLIGLEFKG | FLENIDSYT |