AJ429077.1

Detailed information

Microorganism
Haloarcula marismortui

Taxonomy
Phylum : Stenosarchaea Class : Halobacteria Order : Halobacteriales Family : Haloarculaceae Genus : Haloarcula

Isolation Source
nan

Enzyme Name
Nitrate reductase subunit 2

Protein Information
Pro_GenBank I.D： CAD22070.1 Length：358 aa Protein FASTA_sequence: Link

Information about Article
Reference：Yoshimatsu et al., 2002 Title：Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui Pubmed ID：11959121.0 Pubmed link： Link Full research link： Link Abstract：Genes encoding the NarG and NarH subunits of the molybdo-iron-sulfur enzyme, a nitrate reductase from a denitrifying halophilic euryarchaeota Haloarcula marismortui, were cloned and sequenced. An incomplete cysteine motif reminiscent of that for a [4Fe-4S] cluster binding was found in the NarG subunit, and complete cysteine arrangements for binding one [3Fe-4S] cluster and three [4Fe-4S] clusters were found in the NarH subunit. In conjunction with chemical, electron paramagnetic resonance, and subcellular localization analyses, we firmly establish that the H. marismortui enzyme is a new archaeal member of the known membrane-bound nitrate reductases whose homologs are found in the bacterial domain.

Reference：Yoshimatsu et al., 2002
Title：Sequence and electron paramagnetic resonance analyses of nitrate reductase NarGH from a denitrifying halophilic euryarchaeote Haloarcula marismortui
Pubmed ID：11959121.0
Pubmed link： Link
Full research link： Link
Abstract：Genes encoding the NarG and NarH subunits of the molybdo-iron-sulfur enzyme, a nitrate reductase from a denitrifying halophilic euryarchaeota Haloarcula marismortui, were cloned and sequenced. An incomplete cysteine motif reminiscent of that for a [4Fe-4S] cluster binding was found in the NarG subunit, and complete cysteine arrangements for binding one [3Fe-4S] cluster and three [4Fe-4S] clusters were found in the NarH subunit. In conjunction with chemical, electron paramagnetic resonance, and subcellular localization analyses, we firmly establish that the H. marismortui enzyme is a new archaeal member of the known membrane-bound nitrate reductases whose homologs are found in the bacterial domain.