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B6db activities: mocr

Description mocR-like proteins
Alternative names mocR;
Cofactor Pyridoxal-phosphate.
Proteins that act primarily as transcriptional regulators, but retain an intact aminotransferase domain.
It is unclear whether they also possess a catalytic function (like the MalY subfamily of cystathionine beta-lyase,
In C. glutamicum, genetic data suggest that a protein of the MocR family functions as an aminotransferase in valine biosynthesis. The gene encoding this protein is located upstream of a potential operon of a newly described pyridoxine biosynthetic pathway and when disrupted, gives rise to a pyridoxine auxotrophy.

According to Milano et al. (2015) at least three subgroups (possibly three families) can be distinguished within the MocR sequences.

PDB 5X03;
Organisms -Eubacteria


mocr (0)
Links Enzyme (activities) mocr
BRENDA (activities) mocr
KEGG (pathways) mocr
PLPMDB (PLP mutants) mocr
 Park SA, Park YS, Lee KS (2017) Crystal structure of the C-terminal domain of Bacillus subtilis GabR reveals a closed conformation by γ-aminobutyric acid binding, inducing transcriptional activation Biochem Biophys Res Commun 487 287-291.

 Schulz A, Stöveken N, Binzen IM, Hoffmann T, Heider J, Bremer E (2017) Feeding on compatible solutes: A substrate-induced pathway for uptake and catabolism of ectoines and its genetic control by EnuR Environ Microbiol 19 926-946.

 Tramonti A, Milano T, Nardella C, di Salvo ML, Pascarella S, Contestabile R (2017) Salmonella typhimurium PtsJ is a novel MocR-like transcriptional repressor involved in regulating the vitamin B6 salvage pathway FEBS J 284 466-484.

 Yu Q, Cai H, Zhang Y, He Y, Chen L, Merritt J, Zhang S, Dong Z (2017) Negative Regulation of Ectoine Uptake and Catabolism in Sinorhizobium meliloti: Characterization of the EhuR Gene J Bacteriol 199 e00119-16.

 Milano T, Contestabile R, Lo Presti A, Ciccozzi M, Pascarella S (2015) The aspartate aminotransferase-like domain of Firmicutes MocR transcriptional regulators Comput Biol Chem 58 55-61.

 Okuda K, Kato S, Ito T, Shiraki S, Kawase Y, Goto M, Kawashima S, Hemmi H, Fukada H, Yoshimura T. (2015) Role of the aminotransferase domain in Bacillus subtilis GabR, a pyridoxal 5'-phosphate-dependent transcriptional regulator Mol Microbiol 95 245-57.

 Takenaka T, Ito T, Miyahara I, Hemmi H, Yoshimura T (2015) A new member of MocR/GabR-type PLP-binding regulator of D-alanyl-D-alanine ligase in Brevibacillus brevis FEBS J 282 4201-17.

 Tramonti A, Fiascarelli A, Milano T, di Salvo ML, Nogués I, Pascarella S, Contestabile R (2015) Molecular mechanism of PdxR – a transcriptional activator involved in the regulation of vitamin B6 biosynthesis in the probiotic bacterium Bacillus clausii FEBS J 282 2966-84.

 Belitsky, B.R. (2004) Bacillus subtilis GabR, a Protein with DNA-binding and Aminotransferase Domains, is a PLP-dependent Transcriptional Regulator J Mol Biol 340 655-64.

 McHardy AC, Tauch A, Rückert C, Pühler A, Kalinowski J. (2003) Genome-based analysis of biosynthetic aminotransferase genes of Corynebacterium glutamicum J Biotechnol 104 229-40.

 Rigali, S.; Derouaux, A.; Giannotta, F.; Dusart, J. (2002) Subdivision of the helix-turn-helix GntR family of bacterial regulators in the FadR, HutC, MocR, and YtrA subfamilies J Biol Chem 277 12507-15.

 Chang, Z.; Sun, Y.; He, J.; Vining L.C. (2001) p-Aminobenzoic acid and chloramphenicol biosynthesis in Streptomyces venezuelae: gene sets for a key enzyme, 4-amino-4-deoxychorismate synthase Microbiology 147 2113-21126.

 Magarvey, N.; He, J.; Vining L.C. (2001) The pdx genetic marker adjacent to the chloramphenicol biosynthesis gene cluster in Streptomyces venezuelae ISP5230: functional characterization Microbiology 147 2103-12.

 Rossbach, S.; Kulpa, D. A.; Rossbach, U.; de Bruijn, F. J. (1994) Molecular and genetic characterization of the rhizopine catabolism (mocABRC) genes of Rhizobium meliloti L5-30 Mol Gen Genet 245 11-24.

Articles on mocr
last changed 2017/10/26 14:46

B6db activities