(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) > cellular organisms: NE > Bacteria: NE > Terrabacteria group: NE > Actinobacteria [phylum]: NE > Actinobacteria [class]: NE > Corynebacteriales: NE > Corynebacteriaceae: NE > Corynebacterium: NE > Corynebacterium glutamicum: NE
Warning: This entry is a compilation of different species or line or strain with more than 90% amino acide identity. You can retrieve all strain data
(Below N is a link to NCBI taxonomic web page and E link to ESTHER at designed phylum.) Corynebacterium glutamicum ATCC 14067: N, E.
Corynebacterium glutamicum R: N, E.
Corynebacterium glutamicum ATCC 13032: N, E.
Corynebacterium glutamicum SCgG1: N, E.
Corynebacterium glutamicum Z188: N, E.
Corynebacterium glutamicum S9114: N, E.
Corynebacterium glutamicum K051: N, E.
Corynebacterium glutamicum SCgG2: N, E.
Corynebacterium glutamicum MB001: N, E.
LegendThis sequence has been compared to family alignement (MSA) red => minority aminoacid blue => majority aminoacid color intensity => conservation rate title => sequence position(MSA position)aminoacid rate Catalytic site Catalytic site in the MSA MPTLAPSGQLEIQAIGDVSTEAGAIITNAEIAYHRWGEYRVDKEGRSNVV LIEHALTGDSNAADWWADLLGPGKAINTDIYCVICTNVIGGCNGSTGPGS MHPDGNFWGNRFPATSIRDQVNAEKQFLDALGITTVAAVVLLGGSMGGAR TLEWAAMYPETVGAAAVLAVSARASAWQIGIQSAQIKAIENDHHWHEGNY YESGCNPATGLGAARRIAHLTYRGELEIDERFGTKAQKNENPLGPYRKPD QRFAVESYLDYQADKLVQRFDAGSYVLLTDALNRHDIGRDRGGLNKALES IKVPVLVAGVDTDILYPYHQQEHLSRNLGNLLAMAKIVSPVGHDAFLTES RQMDRIVRNFFSLISPDEDNPSTYIEFYI
References
Title: Rapid identification of unknown carboxyl esterase activity in Corynebacterium glutamicum using RNA-guided CRISPR interference Lee SS, Shin H, Jo S, Lee SM, Um Y, Woo HM Ref: Enzyme Microb Technol, 114:63, 2018 : PubMed
RNA-guided genome engineering technologies have been developed for the advanced metabolic engineering of microbial cells to enhance production of value-added chemicals in Corynebacterium glutamicum as an industrial host. In this study, the RNA-guided CRISPR interference (CRISPRi) was applied to rapidly identify of unknown genes for native esterase activity in C. glutamicum. Combining with the carboxyl esterase (MekB) protein sequence alignment, two target genes (the cg0961 and cg0754) were selected for the CRISPRi application to investigate the possible native esterase in C. glutamicum. The recombinant strain with repressed expression of the cg0961 gene exhibited almost no capability on degradation of methyl acetate as a substrate of carboxyl esterase. This result was also confirmed in the cg0961 gene deletion mutant. Thus, we concluded that Cg0961 plays a major role of the native carboxyl esterase activity in C. glutamicum. In addition, CRISPRi demonstrated an application for gene identification and its function as another genetic tool for metabolic engineering in C. glutamicum.
The complete genome sequence of Corynebacterium glutamicum strain R was determined to allow its comparative analysis with other corynebacteria. The biology of corynebacteria was explored by refining the definition of the subset of genes that constitutes the corynebacterial core as well as those characteristic of saprophytic and pathogenic ecological niches. In addition, the relative scarcity of corynebacterial sigma factors and the plasticity of their two-component system machinery reflect their relatively exacting nutritional requirements and reduced membrane-associated and secreted proteins. The conservation of key genes and pathways between corynebacteria, mycobacteria and Nocardia validates the use of C. glutamicum to study fundamental processes that are conserved in slow-growing mycobacteria, including pathogenesis-associated mechanisms. The discovery of 39 novel genes in C. glutamicum R that have not been previously reported in other corynebacteria supports the rationale for sequencing additional corynebacterial genomes to better define the corynebacterial pan-genome and identify previously undetected metabolic pathways in these organisms.
        
Title: Isolation and analysis of metA, a methionine biosynthetic gene encoding homoserine acetyltransferase in corynebacterium glutamicum Park SD, Lee JY, Kim Y, Kim JH, Lee HS Ref: Mol Cells, 8:286, 1998 : PubMed
The metA gene encoding homoserine acetyltransferase, the first enzyme of the methionine biosynthetic pathway, was isolated from a pMT1-based corynebacterium glutamicum gene library via complementation of an Escherichia coli metA mutant. A DNA-sequence analysis of the cloned DNA is identified an open-reading frame of 1,137 bp which encodes a protein with the molecular weight of 41,380 comprising 379 amino acids. The putative protein product showed good amino acid-sequence homology to its counterpart in other organisms. The internal fragment of the cloned DNA was successfully used to disrupt chromosomal metA, demonstrating the identity of the cloned gene. The C. glutamicum metA mutant lost the ability to grow on glucose minimal medium supplemented with homoserine. However, the mutant could grow on a minimal medium supplemented with cystathionine, demonstrating that C. glutamicum uses the cystathionine route to synthesize methionine. Introduction of a plasmid carrying cloned metA into C. glutamicum resulted in a 10-fold increase in enzyme activities and expression of a protein product of M(r) 41,000, which agrees with the sequence data and is similar in size to those of other homoserine acetyltransferases. Unlike E. coli whose metA product uses succinyl coenzyme A as a substrate, the cloned metA gene produced homoserine acetyltransferase which uses only acetyl coenzyme A as the acyl donor.