HMM Summary Page: TIGR01703

Functionhydroxylamine reductase
Gene Symbolhcp
Trusted Cutoff360.80
Domain Trusted Cutoff360.80
Noise Cutoff181.95
Domain Noise Cutoff181.95
Isology Typeequivalog
EC Number1.7.-.-
HMM Length522
Mainrole CategoryCellular processes
Subrole CategoryDetoxification
AuthorHaft DH
Entry DateSep 25 2002 2:34PM
Last ModifiedDec 12 2011 9:42PM
CommentThis HMM represents a family of proteins containing an unusual 4Fe-2S-2O hydrid cluster. Earlier reports had proposed a 6Fe-6S prismane cluster. This subfamily is heterogeneous with respect to the presence or absence of a region of about 100 amino acids not far from the N-terminus of the protein. Members have been described as monomeric. The general function is unknown, although members from E. coli and several other species have hydroxylamine reductase activity. Members are found in various bacteria, in Archaea, and in several parasitic eukaryotes: Giardia intestinalis, Trichomonas vaginalis, and Entamoeba histolytica.
ReferencesRN [1] RM PMID:12374823 RT Hydroxylamine reductase activity of the hybrid cluster protein from Escherichia coli. RA Wolfe MT, Heo J, Garavelli JS, Ludden PW RL J Bacteriol. 2002 Nov;184(21):5898-902. RN [2] RM PMID:10651802 RT The hybrid-cluster protein ('prismane protein') from Escherichia coli. Characterization of the hybrid-cluster protein, redox properties of the [2Fe-2S] and [4Fe-2S-2O] clusters and identification of an associated NADH oxidoreductase containing FAD and [2Fe-2S]. RA van den Berg WA, Hagen WR, van Dongen WM. RL Eur J Biochem 2000 Feb;267(3):666-76 RN [3] RM PMID:1318832 RT Purification and biochemical characterization of a putative [6Fe-6S] prismane-cluster-containing protein from Desulfovibrio vulgaris (Hildenborough). RA Pierik AJ, Wolbert RB, Mutsaers PH, Hagen WR, Veeger C RL Eur J Biochem. 1992 Jun 15;206(3):697-704. DR HAMAP; MF_00069; 89 of 90