(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 > Streptomycetales: NE > Streptomycetaceae: NE > Streptomyces: NE > Streptomyces clavuligerus: NE
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 MLDAGGTTLSALLAEAQGPPRATLLALHGGGMTAAYFDGQADPALSLLTL GASLGWTVLAVDRPGYGASAETLPDGLPLAEQAVALRHALADFGGRYPLG AGLCVLAHSYGGKLALTAAAQGLHDELLGIEISGCGHRYAADPPAGRPAP FGGPGGPRLNWGPLTLYAPRTFSLAGSVVAPMPLREAVEAARWEGAFRTL AGAVRVPVRMTFAEYEGWWRHDPEALAELTGLLSSVPRLVIERQPGAGHN ISLGWAARAYHLRALGFLEECLQPRLARPASVSASASASASASARAASAP EPIQR
Reference
Title: Genes specific for the biosynthesis of clavam metabolites antipodal to clavulanic acid are clustered with the gene for clavaminate synthase 1 in Streptomyces clavuligerus Mosher RH, Paradkar AS, Anders C, Barton B, Jensen SE Ref: Antimicrobial Agents & Chemotherapy, 43:1215, 1999 : PubMed
Portions of the Streptomyces clavuligerus chromosome flanking cas1, which encodes the clavaminate synthase 1 isoenzyme (CAS1), have been cloned and sequenced. Mutants of S. clavuligerus disrupted in cvm1, the open reading frame located immediately upstream of cas1, were constructed by a gene replacement procedure. Similar techniques were used to generate S. clavuligerus mutants carrying a deletion that encompassed portions of the two open reading frames, cvm4 and cvm5, located directly downstream of cas1. Both classes of mutants still produced clavulanic acid and cephamycin C but lost the ability to synthesize the antipodal clavam metabolites clavam-2-carboxylate, 2-hydroxymethyl-clavam, and 2-alanylclavam. These results suggested that cas1 is clustered with genes essential and specific for clavam metabolite biosynthesis. When a cas1 mutant of S. clavuligerus was constructed by gene replacement, it produced lower levels of both clavulanic acid and most of the antipodal clavams except for 2-alanylclavam. However, a double mutant of S. clavuligerus disrupted in both cas1 and cas2 produced neither clavulanic acid nor any of the antipodal clavams, including 2-alanylclavam. This outcome was consistent with the contribution of both CAS1 and CAS2 to a common pool of clavaminic acid that is shunted toward clavulanic acid and clavam metabolite biosynthesis.
