![]() |
|
PROSITE documentation PDOC00392 [for PROSITE entry PS00932] |
The following proteins belong to the molybdenium (Mo) or tungsten (W) containing enzyme family, the Mo/W bis-MGD (molybdopterin-guanine-dinucleotide) oxydoreductases [1,2,3]:
These proteins range from 715 amino acids (fdhF) to 1246 amino acids (narZ) in size and have been shown to share a number of regions of sequence similarity.
The Mo/W bis-MGD oxydoreductases contains a domain that coordinates a [4Fe-4S] cluster. The cluster is ligated either by four Cys residues or three Cys residues and one His residue [5]. The fold of the Mo/W bis-MGD-type 4Fe-4S domain is of the αβ type and contains three β strands and one α helice (see <PDB:1H0H>) [6].
We derived three signature patterns for these enzymes. The first is based on a conserved region in the N-terminal section and contains three cysteine (histidine) residues that bind [4Fe-4S] cluster. It should be noted that this region is not present in bisC. The second pattern is derived from a conserved region located in the central part of these enzymes. We also developed a profile that covers the entire Mo/W bis-MGD-type 4Fe-4S domain.
Last update:June 2013 / Profile revised.
-------------------------------------------------------------------------------
PROSITE methods (with tools and information) covered by this documentation:
1 | Authors | Wootton J.C. Nicolson R.E. Cock J.M. Walters D.E. Burke J.F. Doyle W.A. Bray R.C. |
Title | Enzymes depending on the pterin molybdenum cofactor: sequence families, spectroscopic properties of molybdenum and possible cofactor-binding domains. | |
Source | Biochim. Biophys. Acta 1057:157-185(1991). | |
PubMed ID | 2015248 |
2 | Authors | Bilous P.T. Cole S.T. Anderson W.F. Weiner J.H. |
Title | Nucleotide sequence of the dmsABC operon encoding the anaerobic dimethylsulphoxide reductase of Escherichia coli. | |
Source | Mol. Microbiol. 2:785-795(1988). | |
PubMed ID | 3062312 |
3 | Authors | Trieber C.A. Rothery R.A. Weiner J.H. |
Title | Multiple pathways of electron transfer in dimethyl sulfoxide reductase of Escherichia coli. | |
Source | J. Biol. Chem. 269:7103-7109(1994). | |
PubMed ID | 8125918 |
4 | Authors | Mejean V. Iobbi-Nivol C. Lepelletier M. Giordano G. Chippaux M. Pascal M.-C. |
Title | TMAO anaerobic respiration in Escherichia coli: involvement of the tor operon. | |
Source | Mol. Microbiol. 11:1169-1179(1994). | |
PubMed ID | 8022286 |
5 | Authors | Rothery R.A. Workun G.J. Weiner J.H. |
Title | The prokaryotic complex iron-sulfur molybdoenzyme family. | |
Source | Biochim. Biophys. Acta 1778:1897-1929(2008). | |
PubMed ID | 17964535 | |
DOI | 10.1016/j.bbamem.2007.09.002 |
6 | Authors | Raaijmakers H. Macieira S. Dias J.M. Teixeira S. Bursakov S. Huber R. Moura J.J. Moura I. Romao M.J. |
Title | Gene sequence and the 1.8 A crystal structure of the tungsten-containing formate dehydrogenase from Desulfovibrio gigas. | |
Source | Structure 10:1261-1272(2002). | |
PubMed ID | 12220497 |