J. Biol. Chem., Vol. 268, Issue 5, 3099-3106, Feb, 1993
Glutamate synthase genes of the diazotroph Azospirillum brasilense. Cloning, sequencing, and analysis of functional domains
R Pelanda, MA Vanoni, M Perego, L Piubelli, A Galizzi, B Curti and G Zanetti
Dipartimento di Fisiologia e Biochimica Generali, Universita degli Studi di Milano, Italy.
A 10-kilobase EcoRI fragment of Azospirillum brasilense genomic DNA was
cloned in Escherichia coli. Two open reading frames of 4548 and 1446 base
pairs (bp) were identified within the fragment as the structural genes for
the alpha and beta subunits (gltB and gltD, respectively) of A. brasilense
GltS. The organization of the gltBD region of A. brasilense differs from
that of the corresponding region in E. coli: in A. brasilense, gltD is
upstream relative to gltB, and its stop codon is separated by 141 bp from
the first ATG of gltB. The deduced amino acid sequences reveal a high
similarity with GltS from E. coli and with the ferredoxin-dependent GltS
from maize. Binding domains for flavin cofactors and NADPH, a domain for
glutamine binding and activation, and cysteine clusters for iron-sulfur
centers formation were tentatively identified on the basis of sequence
comparison with flavoproteins, pyridine nucleotide-dependent enzymes,
amidotransferases, and iron- sulfur proteins.
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