Cloning, characterization, and expression of a novel gene encoding a reversible 4-hydroxybenzoate decarboxylase from Clostridium hydroxybenzoicum.
A novel gene, designated ohb1, which encodes the oxygen-sensitive and biotin-, ATP-, thiamin-, pyridoxal phosphate-, and metal-ion-independent, reversible 4-hydroxybenzoate decarboxylase (4-HOB-DC) from the obligate anaerobe Clostridium hydroxybenzoicum JW/Z-1(T) was sequenced (GenBank accession no. AF128880) and expressed. The 1,440-bp open reading frame (ORF) (ohb1) encodes 480 amino acids. Major properties of the heterologous enzyme (Ohb1) expressed in Escherichia coli DH5alpha were the same as those described for the native 4-HOB-DC (Z. He and J. Wiegel, J. Bacteriol. 178:3539-3543, 1996). The deduced amino acid sequence shows up to 57% identity and up to 74% similarity to hypothetical proteins deduced from ORFs in genomes from bacteria and archaea, suggesting a possible novel gene family.
Huang
J
J
Department of Microbiology and Center for Biological Resource Recovery, University of Georgia, Athens, Georgia 30602-2605, USA.
He
Z
Z
Wiegel
J
J
D001483:Base Sequence; D002262:Carboxy-Lyases / Q000235:genetics* / Q000378:metabolism; D003001:Cloning, Molecular; D003013:Clostridium / Q000201:enzymology* / Q000235:genetics*; D015964:Gene Expression Regulation, Bacterial; D015971:Gene Expression Regulation, Enzymologic; D008969:Molecular Sequence Data; D011401:Promoter Regions, Genetic / Q000235:genetics; D017386:Sequence Homology, Amino Acid
D002262:Carboxy-Lyases; C065828:4-hydroxybenzoate decarboxylase