P83589
Gene name |
DR_2477 |
Protein name |
Probable 3-hydroxyacyl-CoA dehydrogenase |
Names |
|
Species |
Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422) |
KEGG Pathway |
|
EC number |
1.1.1.35: 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 P83589
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P83589-F1 | Predicted | AlphaFoldDB |
No variants for P83589
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P83589 | |||||
No associated diseases with P83589
Functions
| Description | ||
|---|---|---|
| EC Number | 1.1.1.35 | With NAD(+) or NADP(+) as acceptor |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| 3-hydroxyacyl-CoA dehydrogenase activity | Catalysis of the reaction: (S)-3-hydroxyacyl-CoA + NAD+ = 3-oxoacyl-CoA + NADH + H(+). |
| 3-hydroxybutyryl-CoA dehydrogenase activity | Catalysis of the reaction: (S)-3-hydroxybutanoyl-CoA + NADP+ = 3-acetoacetyl-CoA + NADPH + H+. |
| NAD+ binding | Binding to the oxidized form, NAD, of nicotinamide adenine dinucleotide, a coenzyme involved in many redox and biosynthetic reactions. |
| oxidoreductase activity | Catalysis of an oxidation-reduction (redox) reaction, a reversible chemical reaction in which the oxidation state of an atom or atoms within a molecule is altered. One substrate acts as a hydrogen or electron donor and becomes oxidized, while the other acts as hydrogen or electron acceptor and becomes reduced. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| fatty acid beta-oxidation | A fatty acid oxidation process that results in the complete oxidation of a long-chain fatty acid. Fatty acid beta-oxidation begins with the addition of coenzyme A to a fatty acid, and occurs by successive cycles of reactions during each of which the fatty acid is shortened by a two-carbon fragment removed as acetyl coenzyme A; the cycle continues until only two or three carbons remain (as acetyl-CoA or propionyl-CoA respectively). |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MKIKKAAVIG | AGVMGAAIAA | QLANAGIPVL | LLDIVLPDKP | DRNFLAKAGV | ERALKARPAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FMDNDRARLI | EVGNLEDDLK | KLKDVDWVLE | AIIEKLDAKH | DLWEKVEKVV | KKTAIISSNS |
| 130 | 140 | 150 | 160 | 170 | 180 |
| SGIPMHLQIE | GRSEDFQRRF | VGAHFFNPPR | YLHLLEVIPT | DKTDPQVVKD | FSEFAEHTLG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| KGVVVANDVP | GFVANRIGVY | GIVRAMQHME | KYGLTPAEVD | QLTGPALGRA | SSATFRTADL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| SGLDIISHVA | TDIGGVTPDD | EDFTLTESFK | NMVAGGILGD | KSGSGFYKKT | KDEKARPRFS |
| 310 | 320 | 330 | 340 | ||
| TTCKPANTKT | RARCACPPWT | PRANLSPSAT | PCTPWKARKA | TSCAPP |