D7UNT2
Gene name |
lcdH (Rs-cdh) |
Protein name |
L-carnitine dehydrogenase |
Names |
CDH, L-CDH |
Species |
Rhizobium sp |
KEGG Pathway |
|
EC number |
1.1.1.108: With NAD(+) or NADP(+) as acceptor |
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 D7UNT2
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-D7UNT2-F1 | Predicted | AlphaFoldDB |
No variants for D7UNT2
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for D7UNT2 | |||||
No associated diseases with D7UNT2
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.108 | With NAD(+) or NADP(+) as acceptor |
| 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. |
3 GO annotations of molecular function
| Name | Definition |
|---|---|
| carnitine 3-dehydrogenase activity | Catalysis of the reaction: carnitine + NAD(+) = 3-dehydrocarnitine + H(+) + NADH. |
| NAD binding | Binding to nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NAD+, or the reduced form, NADH. |
| NAD+ binding | Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. |
2 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. |
| fatty acid metabolic process | The chemical reactions and pathways involving fatty acids, aliphatic monocarboxylic acids liberated from naturally occurring fats and oils by hydrolysis. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSFITKAACV | GGGVIGGAWV | ARFALAGIDV | KIFDPHPEAE | RIIGEVMANA | ERAYAMLTMA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PLPPKGKLTF | CKSIEEAVEG | ADWIQESVPE | RLELKRGVIT | KIDAAARPDA | LIGSSTSGLL |
| 130 | 140 | 150 | 160 | 170 | 180 |
| PSDLQSEMHH | PERMFVAHPY | NPVYLLPLVE | LVGGKKTSKA | TIERAMQGVE | QIGMKGVVIA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KEIEAFVGDR | LLEALWREAL | WLIQDDICHT | ETLDNVMRYS | FGMRWAQMGL | FETYRIAGGE |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AGMRHFLAQF | GPCLKWPWTK | FTDVVDLDDA | LVEKIGAQSD | AQAAGRSIRE | LERIRDENLV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GIMHALKSGN | GGEGWGAGKL | LADFEAKLWA | NARKPEADLG | DVKPLRILDT | KVSAAWVDYN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| GHMTEHRYLQ | VFGDTSDGVL | RLIGVDLDYV | RDGHSYYTVE | THIRNLGDEA | SGEALYSTCQ |
| 430 | 440 | 450 | 460 | 470 | 480 |
| ILSSDEKRLH | IFSTIYNAAT | NEAVATAEQM | MLHVDSKAGK | AVAAPEAVLS | KLRAITEAHA |
| 490 | |||||
| QLQTPDGAGR | FVGQKRA |