Accession | TIGR01755 |
Name | flav_wrbA |
Function | NAD(P)H:quinone oxidoreductase, type IV |
Gene Symbol | wrbA |
Trusted Cutoff | 132.50 |
Domain Trusted Cutoff | 132.50 |
Noise Cutoff | 121.15 |
Domain Noise Cutoff | 121.15 |
Isology Type | equivalog |
EC Number | 1.6.5.2 |
HMM Length | 197 |
Mainrole Category | Energy metabolism |
Subrole Category | Electron transport |
Gene Ontology Term | GO:0003955: NAD(P)H dehydrogenase (quinone) activity molecular_function |
| GO:0055114: oxidation-reduction process biological_process |
Author | Haft DH |
Entry Date | Nov 25 2002 5:02PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This HMM represents a protein, WrbA, related to and slightly larger than flavodoxin. It was just shown, in E. coli and Archaeoglobus fulgidus (and previously for some eukaryotic homologs) to act as fourth type of NAD(P)H:quinone oxidoreductase. In E. coli, this protein was earlier reported to be produced during stationary phase, bind to the trp repressor, and make trp operon repression more efficient. WrbA does not interact with the trp operator by itself. Members are found in species in which homologs of the E. coli trp operon repressor TrpR (SP:P03032) are not detected. |
References | RN [1]
RM PMID: 16672604
RT WrbA from Escherichia coli and Archaeoglobus fulgidus is an NAD(P)H:quinone oxidoreductase.
RA Patridge EV, Ferry JG
RL J Bacteriol. 2006 May;188(10):3498-506.
RN [2]
RM PMID: 9694845
RT Biochemical characterization of WrbA, founding member of a new family of multimeric flavodoxin-like proteins.
RA Grandori R, Khalifah P, Boice JA, Fairman R, Giovanielli K, Carey J
RL J Biol Chem. 1998 Aug 14;273(33):20960-6.
RN [3]
RM 8516330
RT A stationary-phase protein of Escherichia coli that affects the mode of association between the trp repressor protein and operator-bearing DNA.
RA Yang W, Ni L, Somerville RL
RL Proc Natl Acad Sci U S A 1993 Jun 15;90(12):5796-800
DR HAMAP; MF_01017; 83 of 85 |