Novel types of two-domain multi-copper oxidases: possible missing links in the evolution.
An analysis of the genome sequence database revealed novel types of two-domain multi-copper oxidases. The two-domain proteins have the conspicuous combination of blue-copper and inter-domain trinuclear copper binding residues, which is common in ceruloplasmin and ascorbate oxidase but not in nitrite reductase, and therefore are considered to retain the characteristics of the plausible ancestral form of ceruloplasmin and ascorbate oxidase. A possible evolutionary relationship of these proteins is proposed.
Graduate School of Information Science, Nara Institute of Science and Technology, 8916-5 Takayama-cho, Ikoma, 630-0101 Nara, Japan. kenske@is.aist-nara.ac.jp
Kensuke
K
Nakamura
Takeshi
T
Kawabata
Kei
K
Yura
Nobuhiro
N
Go
D000595:Amino Acid Sequence; D001204:Ascorbate Oxidase / Q000737:chemistry / Q000235:genetics; D001665:Binding Sites; D002570:Ceruloplasmin / Q000737:chemistry / Q000235:genetics; D017124:Conserved Sequence; D003300:Copper / Q000737:chemistry / Q000378:metabolism; D019143:Evolution, Molecular; D008969:Molecular Sequence Data; D009572:Nitrite Reductases / Q000737:chemistry / Q000235:genetics; D010088:Oxidoreductases / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D010802:Phylogeny; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid
D003300:Copper; D010088:Oxidoreductases; D001204:Ascorbate Oxidase; C024748:copper oxidase; D002570:Ceruloplasmin; D009572:Nitrite Reductases