P0A8G6

PR
Gene name
wrbA (b1004, JW0989)
Protein name
NAD(P)H dehydrogenase (quinone)
Names
Flavoprotein WrbA, NAD(P)H:quinone oxidoreductase, NQO
Species
Escherichia coli (strain K12)
KEGG Pathway
eco:b1004
EC number
1.6.5.2: 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)

132-198 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

11 structures for P0A8G6

Entry ID Method Resolution Chain Position Source
2R96 X-ray 260 A A/C 1-198 PDB
2R97 X-ray 200 A A/C 1-198 PDB
2RG1 X-ray 185 A A/B 1-198 PDB
3B6I X-ray 166 A A/B 1-198 PDB
3B6J X-ray 205 A A/B 1-198 PDB
3B6K X-ray 199 A A/B 1-198 PDB
3B6M X-ray 185 A A/B 1-198 PDB
3ZHO X-ray 120 A A/B 2-198 PDB
4YQE X-ray 133 A A/B 2-198 PDB
5F12 X-ray 150 A A/B 2-198 PDB
AF-P0A8G6-F1 Predicted AlphaFoldDB

No variants for P0A8G6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for P0A8G6

No associated diseases with P0A8G6

2 regional properties for P0A8G6

Type Name Position InterPro Accession
domain NADPH-dependent FMN reductase-like 4 - 143 IPR005025
domain Flavodoxin/nitric oxide synthase 4 - 189 IPR008254

Functions

Description
EC Number 1.6.5.2 With a quinone or similar compound 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
cytosol The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes.
membrane A lipid bilayer along with all the proteins and protein complexes embedded in it an attached to it.
protein-containing complex A stable assembly of two or more macromolecules, i.e. proteins, nucleic acids, carbohydrates or lipids, in which at least one component is a protein and the constituent parts function together.

8 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.
identical protein binding Binding to an identical protein or proteins.
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.
NADH dehydrogenase (quinone) activity Catalysis of the reaction: NADH + H+ + a quinone = NAD+ + a quinol.
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.
NADPH dehydrogenase (quinone) activity Catalysis of the reaction: NADPH + H+ + a quinone = NADP+ + a quinol.

1 GO annotations of biological process

Name Definition
response to oxidative stress Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MAKVLVLYYS MYGHIETMAR AVAEGASKVD GAEVVVKRVP ETMPPQLFEK AGGKTQTAPV
70 80 90 100 110 120
ATPQELADYD AIIFGTPTRF GNMSGQMRTF LDQTGGLWAS GALYGKLASV FSSTGTGGGQ
130 140 150 160 170 180
EQTITSTWTT LAHHGMVIVP IGYAAQELFD VSQVRGGTPY GATTIAGGDG SRQPSQEELS
190
IARYQGEYVA GLAVKLNG