SMART: Pfam domain Nitrate_red

Nitrate_red_del

PFAM accession number:	PF02613
Interpro abstract (IPR020945):	This entry represents a family of proteins which are involved in enzymes assembly and/or maturation: The TorD protein is involved in the maturation of the the trimethylamine N-oxide reductase TorA (a DMSO reductase family member) in Escherichia coli [ (PUBMED:12766163) ]. TorA is a molybdenum-containing enzyme which requires the the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. TorD acts as a chaperone, binding to apoTorA and promoting efficient incorporation of the cofactor into the protein. Nitrate reductase delta subunit (NarJ). This subunit is not part of the nitrate reductase enzyme but is a chaperone required for proper molybdenum cofactor insertion and final assembly of the nitrate reductase [ (PUBMED:1732220) (PUBMED:9305880) (PUBMED:9632249) ]. NarJ exhibits sequence homology to chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation [ (PUBMED:16540088) ]. The archetypal Tat proofreading chaperones belong to the TorD family [ (PUBMED:22289056) ]. Twin-arginine leader-binding protein DmsD, which could be required for the biogenesis of DMSO reductase rather than for the targeting of DmsA to the inner membrane [ (PUBMED:12527378) (PUBMED:12813051) (PUBMED:20169075) ]. Dimethyl sulphide dehydrogenase protein DdhD. This protein is thought to function as chaperone protein in the assembly of an active dimethyl sulphide dehydrogenase DdhABC [ (PUBMED:12067345) ].

PFAM accession number:

PF02613

Interpro abstract (IPR020945):

This entry represents a family of proteins which are involved in enzymes assembly and/or maturation:

The TorD protein is involved in the maturation of the the trimethylamine N-oxide reductase TorA (a DMSO reductase family member) in Escherichia coli [ (PUBMED:12766163) ]. TorA is a molybdenum-containing enzyme which requires the the insertion of a bis(molybdopterin guanine dinucleotide) molybdenum (bis(MGD)Mo) cofactor in its catalytic site to be active and translocated to the periplasm. TorD acts as a chaperone, binding to apoTorA and promoting efficient incorporation of the cofactor into the protein.
Nitrate reductase delta subunit (NarJ). This subunit is not part of the nitrate reductase enzyme but is a chaperone required for proper molybdenum cofactor insertion and final assembly of the nitrate reductase [ (PUBMED:1732220) (PUBMED:9305880) (PUBMED:9632249) ]. NarJ exhibits sequence homology to chaperones involved in maturation and cofactor insertion of E. coli redox enzymes that are mediated by twin-arginine translocase (Tat) dependent translocation [ (PUBMED:16540088) ]. The archetypal Tat proofreading chaperones belong to the TorD family [ (PUBMED:22289056) ].
Twin-arginine leader-binding protein DmsD, which could be required for the biogenesis of DMSO reductase rather than for the targeting of DmsA to the inner membrane [ (PUBMED:12527378) (PUBMED:12813051) (PUBMED:20169075) ].
Dimethyl sulphide dehydrogenase protein DdhD. This protein is thought to function as chaperone protein in the assembly of an active dimethyl sulphide dehydrogenase DdhABC [ (PUBMED:12067345) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Nitrate_red_del