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PROSITE documentation PDOC01009 |
A number of proteins involved in the biosynthesis of metallo cofactors have been shown [1,2] to be evolutionary related. These proteins are:
All these proteins share, in their N-terminal region, a conserved domain that contains three cysteines. In moaA, these cysteines have been shown [1] to be important for the biological activity. They could be inolved in the binding of an iron-sulfur cluster.
Expert(s) to contact by email: Last update:May 2004 / Text revised.
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PROSITE method (with tools and information) covered by this documentation:
1 | Authors | Menendez C. Igloi G. Henninger H. Brandsch R. |
Title | A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter nicotinovorans: characterization and site-directed mutagenesis of the encoded protein. | |
Source | Arch. Microbiol. 164:142-151(1995). | |
PubMed ID | 8588735 |
2 | Authors | Hoff T. Schnorr K.M. Meyer C. Caboche M. |
Title | Isolation of two Arabidopsis cDNAs involved in early steps of molybdenum cofactor biosynthesis by functional complementation of Escherichia coli mutants. | |
Source | J. Biol. Chem. 270:6100-6107(1995). | |
PubMed ID | 7890743 |