C1I202
Gene name |
pnpB |
Protein name |
p-benzoquinone reductase |
Names |
NAD(P)H dehydrogenase (quinone) |
Species |
Pseudomonas sp (strain WBC-3) |
KEGG Pathway |
ag:ABU50909 |
EC number |
1.6.5.6: With a quinone or similar compound 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
3 structures for C1I202
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 4LA4 | X-ray | 207 A | A/B | 1-207 | PDB |
| 4LAF | X-ray | 176 A | A/B/C/D | 1-207 | PDB |
| AF-C1I202-F1 | Predicted | AlphaFoldDB |
No variants for C1I202
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for C1I202 | |||||
No associated diseases with C1I202
4 regional properties for C1I202
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | DNA-directed DNA polymerase, family B, exonuclease domain | 29 - 194 | IPR006133-1 |
| domain | DNA-directed DNA polymerase, family B, exonuclease domain | 197 - 291 | IPR006133-2 |
| domain | DNA-directed DNA polymerase, family B, multifunctional domain | 357 - 759 | IPR006134 |
| conserved_site | DNA-directed DNA polymerase, family B, conserved site | 543 - 551 | IPR017964 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.6.5.6 | With a quinone or similar compound 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 |
6 GO annotations of molecular function
| Name | Definition |
|---|---|
| flavin adenine dinucleotide binding | Binding to FAD, flavin-adenine dinucleotide, the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes, in either the oxidized form, FAD, or the reduced form, FADH2. |
| FMN binding | Binding to flavin mono nucleotide. Flavin mono nucleotide (FMN) is the coenzyme or the prosthetic group of various flavoprotein oxidoreductase enzymes. |
| 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(P)H dehydrogenase (quinone) activity | Catalysis of the reaction: NAD(P)H + H+ + a quinone = NAD(P)+ + a hydroquinone. |
| NADP binding | Binding to nicotinamide-adenine dinucleotide phosphate, a coenzyme involved in many redox and biosynthetic reactions; binding may be to either the oxidized form, NADP+, or the reduced form, NADPH. |
| p-benzoquinone reductase (NADPH) activity | Catalysis of the reaction: 1,4-benzoquinone + H(+) + NADPH = hydroquinone + NADP(+). |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| 4-nitrophenol catabolic process | The chemical reactions and pathways resulting in the breakdown of 4-nitrophenol, a nitroaromatic compound which is used in the production of dyes, leather treatment agents, fungicides and as an intermediate in the production of the insecticide parathion. |
| aromatic compound catabolic process | The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MPTKIQIVFY | SSYGHIYKMA | EAIAAGAREV | GDVEVTLLQV | PELMPEEVQV | KSGIKGYRAA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| FGSIPYATPE | VLAEADAIIF | GTPTRFGNMC | SQMRNFLDQT | GGLWMSGGLI | GKVGSVFTST |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ASQHGGQETT | ITSFHTTLLH | HGMVIVGVPY | SEPGLTNMTE | ISGGTPYGAS | TLAGADGSRQ |
| 190 | 200 | ||||
| PSENELQIAR | FQGKHVATIA | KRLANNK |