Journal of Bacteriology, August 1999, p. 5119-5122, Vol. 181, No. 16
0021-9193/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

andDepartment of Microbiology and Center for Biological Resource Recovery, University of Georgia, Athens, Georgia 30602-2605
Received 1 March 1999/Accepted 2 June 1999
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-1T 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 DH5
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.
Present address: Department of Biochemistry Center for Biomolecular
Structure Analysis, University of Texas Health Science Center at San
Antonio, San Antonio, TX 78284.
Present address: Air Force Research Lab, Tyndall Air Force Base,
FL 32403-5323.
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