Q9UR35
Gene name |
CBR1 |
Protein name |
NADH-cytochrome b5 reductase 1 |
Names |
Microsomal cytochrome b reductase |
Species |
Mortierella alpina (Oleaginous fungus) (Mortierella renispora) |
KEGG Pathway |
|
EC number |
1.6.2.2: With a heme protein 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 Q9UR35
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q9UR35-F1 | Predicted | AlphaFoldDB |
No variants for Q9UR35
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q9UR35 | |||||
No associated diseases with Q9UR35
5 regional properties for Q9UR35
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | TolB, N-terminal | 21 - 127 | IPR007195 |
| repeat | WD40-like beta propeller | 243 - 270 | IPR011659-1 |
| repeat | WD40-like beta propeller | 281 - 315 | IPR011659-2 |
| repeat | WD40-like beta propeller | 324 - 348 | IPR011659-3 |
| repeat | WD40-like beta propeller | 377 - 400 | IPR011659-4 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.6.2.2 | With a heme protein as acceptor |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| endoplasmic reticulum membrane | The lipid bilayer surrounding the endoplasmic reticulum. |
| integral component of membrane | The component of a membrane consisting of the gene products and protein complexes having at least some part of their peptide sequence embedded in the hydrophobic region of the membrane. |
| mitochondrial outer membrane | The outer, i.e. cytoplasm-facing, lipid bilayer of the mitochondrial envelope. |
2 GO annotations of molecular function
| Name | Definition |
|---|---|
| cytochrome-b5 reductase activity, acting on NAD(P)H | Catalysis of the reaction: NAD(P)H + H+ + 2 ferricytochrome b(5) = NAD(P)+ + 2 ferrocytochrome b(5). |
| NADH dehydrogenase activity | Catalysis of the reaction: NADH + H+ + acceptor = NAD+ + reduced acceptor. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| peptidyl-diphthamide biosynthetic process from peptidyl-histidine | The modification of peptidyl-histidine to 2'-(3-carboxamido-3-(trimethylammonio)propyl)-L-histidine, known as diphthamide, found in translation elongation factor EF-2. The process occurs in eukaryotes and archaea but not eubacteria. |
| tRNA wobble base 5-methoxycarbonylmethyl-2-thiouridinylation | The process whereby a wobble base uridine residue in a tRNA is modified to 5-methoxycarbonylmethyl-2-thiouridine. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MTLSNPAIAA | ASGVILAGAY | LIDPSALPFV | AAGVAATWAR | VLFKKTAVKT | PPMDPKEYRK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FKLVDKVHCS | PNTAMYKFAL | PHEDDLLNLP | IGQHISIMAN | INGKDISRSY | TPTSSSDDVG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| HFVLCIKSYP | QGNISKMFSE | LSIGDSINAR | GPKGQFSYTP | NMCRAIGMIA | GGTGLTPMLQ |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IIRAIVKNPE | DKTQVNFIFA | NVTEEDIILK | AELDLLSQKH | PQFKVYYVLN | NAPEGWTGGV |
| 250 | 260 | 270 | 280 | 290 | |
| GFVNADMIKE | HMPAPAADIK | VLLCGPPPMV | SAMSKITQDL | GYDKVNAVSK | LPDQVFKF |