A Corynebacterium glutamicum gene encoding a two-domain protein similar to biotin carboxylases and biotin-carboxyl-carrier proteins.
Following the analysis of transposon Tn5432-induced mutants of Corynebacterium glutamicum ATCC 13032, a gene encoding a protein with a biotin-binding motif was cloned. The DNA sequence of this gene revealed an open reading frame encoding 591 amino acids with a calculated mol. mass of 63.4 kDa. The protein is composed of two domains, an N-terminal biotin carboxylase and a C-terminal biotin-carboxyl-carrier protein, that are highly similar to corresponding subunits from prokaryotic and eukaryotic biotin enzymes. Over 70% identity was found to a protein from Mycobacterium leprae proposed to be part of an acyl-CoA carboxylase. Since it was not possible to inactivate the C. glutamicum gene, the gene most likely encodes a subunit of the essential acetyl-CoA carboxylase, which catalyzes the committed step in fatty acid synthesis.
Jäger
W
W
Lehrstuhl für Genetik, Universität Bielefeld, Postfach 100131, D-33501 Bielefeld, Germany.
Peters-Wendisch
P G
PG
Kalinowski
J
J
Pühler
A
A
D000595:Amino Acid Sequence; D019731:Carbon-Nitrogen Ligases; D002352:Carrier Proteins / Q000235:genetics*; D003001:Cloning, Molecular; D003352:Corynebacterium / Q000235:genetics*; D005798:Genes, Bacterial / Q000235:genetics*; D008025:Ligases / Q000235:genetics*; D008969:Molecular Sequence Data; D009166:Mycobacterium leprae / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D002352:Carrier Proteins; C017071:biotin-binding proteins; D008025:Ligases; D019731:Carbon-Nitrogen Ligases; C019791:biotin carboxylase