{PDOC01009}
{PS01305; MOAA_NIFB_PQQE}
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* moaA / nifB / pqqE family signature *
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A number  of  proteins  involved in the biosynthesis of metallo cofactors have
been shown [1,2] to be evolutionary related. These proteins are:

 - Bacterial  and  archebacterial  protein  moaA,  which  is  involved  in the
   biosynthesis of the molybdenum cofactor (molybdopterin; MPT).
 - Arabidopsis thaliana cnx2, a protein involved in molybdopterin biosynthesis
   and which is highlys similar to moaA.
 - Bacillus  subtilis  narA,  which  seems  to  be  the  moaA ortholog in that
   bacteria.
 - Bacterial  protein  nifB (or fixZ) which is involved in the biosynthesis of
   the nitrogenase iron-molybdenum cofactor.
 - Bacterial  protein  pqqE  which  is  involved  in  the  biosynthesis of the
   cofactor pyrrolo-quinoline-quinone (PQQ).
 - Pyrococcus  furiosus  cmo,  a  protein  involved  in  the  synthesis  of  a
   molybdopterin-based tungsten cofactor.
 - Caenorhabditis elegans hypothetical protein F49E2.1.

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.

-Consensus pattern: [LIV]-x(3)-C-[NDP]-[LIVMF]-[DNQRS]-C-x-[FYM]-C
                    [The 3 C's may be Fe-S ligands]
-Sequences known to belong to this class detected by the pattern: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.

-Expert(s) to contact by email:
           Menendez C.; menendez@ruf.uni-freiburg.de

-Last update: May 2004 / Text revised.

[ 1] Menendez C., Igloi G., Henninger H., Brandsch R.
     "A pAO1-encoded molybdopterin cofactor gene (moaA) of Arthrobacter
     nicotinovorans: characterization and site-directed mutagenesis of the
     encoded protein."
     Arch. Microbiol. 164:142-151(1995).
     PubMed=8588735
[ 2] Hoff T., Schnorr K.M., Meyer C., Caboche M.
     "Isolation of two Arabidopsis cDNAs involved in early steps of
     molybdenum cofactor biosynthesis by functional complementation of
     Escherichia coli mutants."
     J. Biol. Chem. 270:6100-6107(1995).
     PubMed=7890743

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