P31572
Gene name |
caiB |
Protein name |
L-carnitine CoA-transferase |
Names |
Crotonobetainyl-CoA:carnitine CoA-transferase |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b0038 |
EC number |
2.8.3.21: CoA-transferases |
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
8 structures for P31572
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1XA3 | X-ray | 185 A | A/B | 2-405 | PDB |
| 1XA4 | X-ray | 190 A | A/B | 2-405 | PDB |
| 1XK6 | X-ray | 185 A | A/B/C/D | 1-405 | PDB |
| 1XK7 | X-ray | 160 A | A/B/C | 1-405 | PDB |
| 1XVT | X-ray | 230 A | A | 1-405 | PDB |
| 1XVU | X-ray | 240 A | A | 1-405 | PDB |
| 1XVV | X-ray | 240 A | A | 1-405 | PDB |
| AF-P31572-F1 | Predicted | AlphaFoldDB |
2 variants for P31572
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| 187 | V>A | strain: O44:K74 [UniProt] | No | ||
| 302 | T>A | strain: O44:K74 [UniProt] | No |
No associated diseases with P31572
No regional properties for P31572
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| No domain, repeats, and functional sites for P31572 | |||
Functions
| Description | ||
|---|---|---|
| EC Number | 2.8.3.21 | CoA-transferases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytoplasm | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. |
1 GO annotations of molecular function
| Name | Definition |
|---|---|
| L-carnitine CoA-transferase activity | Catalysis of the reactions: (E)-4-(trimethylammonio)but-2-enoyl-CoA + L-carnitine = (E)-4-(trimethylammonio)but-2-enoate + L-carnitinyl-CoA and 4-trimethylammoniobutanoyl-CoA + L-carnitine = 4-trimethylammoniobutanoate + L-carnitinyl-CoA. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| carnitine catabolic process | The chemical reactions and pathways resulting in the breakdown of carnitine (hydroxy-trimethyl aminobutyric acid), a compound that participates in the transfer of acyl groups across the inner mitochondrial membrane. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MDHLPMPKFG | PLAGLRVVFS | GIEIAGPFAG | QMFAEWGAEV | IWIENVAWAD | TIRVQPNYPQ |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSRRNLHALS | LNIFKDEGRE | AFLKLMETTD | IFIEASKGPA | FARRGITDEV | LWQHNPKLVI |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AHLSGFGQYG | TEEYTNLPAY | NTIAQAFSGY | LIQNGDVDQP | MPAFPYTADY | FSGLTATTAA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LAALHKVRET | GKGESIDIAM | YEVMLRMGQY | FMMDYFNGGE | MCPRMSKGKD | PYYAGCGLYK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CADGYIVMEL | VGITQIEECF | KDIGLAHLLG | TPEIPEGTQL | IHRIECPYGP | LVEEKLDAWL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ATHTIAEVKE | RFAELNIACA | KVLTVPELES | NPQYVARESI | TQWQTMDGRT | CKGPNIMPKF |
| 370 | 380 | 390 | 400 | ||
| KNNPGQIWRG | MPSHGMDTAA | ILKNIGYSEN | DIQELVSKGL | AKVED |