EC Number |
Subunits |
Reference |
---|
1.3.7.7 | heterodimer |
1 * 38000 + 1 * 49000 + 1 * 58000, SDS-PAGE |
672764 |
1.3.7.7 | heterooctamer |
(alpha2)2(betagamma)4, DPOR is a nitrogenase-like enzyme consisting of two components, L-protein, a BchL dimer, and NB-protein, a BchN-BchB heterotetramer, which are structurally related to nitrogenase Fe protein and MoFe protein, respectively |
-, 713102 |
1.3.7.7 | heterooctamer |
(alpha2)2(betagamma)4, DPOR is composed of the subunits ChlL, ChlN, and ChlB. Homodimeric ChlL2 bearing an intersubunit [4Fe-4S] cluster is an ATP-dependent reductase transferring single electrons to the heterotetrameric (ChlN/ChlB)2 complex. The latter contains two intersubunit [4Fe-4S] clusters and two protochlorophyllide binding sites, respectively, structure analysis of the catalytic (ChlN/ChlB)2 complex, overview. Subunits ChlN and ChlB exhibit a related architecture of three subdomains each built around a central, parallel beta-sheet surrounded by alpha-helices. Two ChlL2 dimers simultaneously interact with the (ChlN/ChlB)2 tetramer, giving rise to a heterooctameric holoenzyme |
712465 |
1.3.7.7 | heterotetramer |
2 * 48671 + 2 * 57191, subunit BchN and subunit BchB, calculated from amino acid sequence |
672324 |
1.3.7.7 | heterotetramer |
2 * 51000 + 2 * 43000 , NB-protein of DPOR, SDS-PAGE |
393862 |
1.3.7.7 | heterotetramer |
2 * 52000 + 2 * 60000, NB-protein complex, SDS-PAGE |
672324 |
1.3.7.7 | heterotetramer |
2 * 57191 + 2 * 46038, NB-protein of DPOR, calculated from amino acid sequence |
393862 |
1.3.7.7 | homodimer |
2 * 31000, L-protein of DPOR, SDS-PAGE |
393862 |
1.3.7.7 | homodimer |
2 * 33413, L-protein of DPOR, calculated from amino acid sequence |
393862 |
1.3.7.7 | homodimer |
2 * 36000, S-tag subunit BchL, SDS-PAGE |
672324 |