Cloning and sequence analysis of the hemB gene of Rhodothermus marinus.
A Rhodothermus marinus gene, hemB, coding for 5-aminolevulinic acid (ALA) dehydratase (ALAD) has been cloned and sequenced. The reading frame of the hemB gene is 1020 base pairs encoding a protein of 340 amino acids with a calculated molecular mass of 37.4 kDa. The amino acid sequence shows homology with eubacterial and eukaryotic ALA dehydratases. A putative metal-binding site of the protein shows strongest homology with corresponding sites from plant ALA dehydratases that require Mg2+ for activity. It differs with respect to only one amino acid out of 20 from a corresponding site in pea ALAD.
Laboratory of Molecular Genetics, Institute of Biology, University of Iceland, IS-108 Reykjavík, Iceland.
K
K
Gudmundsdóttir
E
E
Sigurdsson
S I
SI
Thorbjarnardóttir
G
G
Eggertsson
D000595:Amino Acid Sequence; D003001:Cloning, Molecular; D004269:DNA, Bacterial / Q000235:genetics; D005798:Genes, Bacterial; D006088:Gram-Negative Aerobic Bacteria / Q000201:enzymology* / Q000235:genetics; D008969:Molecular Sequence Data; D000623:Porphobilinogen Synthase / Q000235:genetics* / Q000378:metabolism; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D004269:DNA, Bacterial; D000623:Porphobilinogen Synthase