| Accession | TIGR01278 |
| Name | DPOR_BchB |
| Function | light-independent protochlorophyllide reductase, B subunit |
| Gene Symbol | bchB |
| Trusted Cutoff | 490.35 |
| Domain Trusted Cutoff | 490.35 |
| Noise Cutoff | 115.30 |
| Domain Noise Cutoff | 115.30 |
| Isology Type | equivalog |
| EC Number | 1.3.7.7 |
| HMM Length | 512 |
| Mainrole Category | Biosynthesis of cofactors, prosthetic groups, and carriers |
| Subrole Category | Chlorophyll and bacteriochlorphyll |
| Gene Ontology Term | GO:0015995: chlorophyll biosynthetic process biological_process |
| | GO:0016491: oxidoreductase activity molecular_function |
| Author | Haft DH |
| Entry Date | Jun 21 2001 11:55AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | Alternate name: dark protochlorophyllide reductase
This enzyme describes the B subunit of the dark form protochlorophyllide reductase, a nitrogenase-like enzyme. This subunit shows homology to the nitrogenase molybdenum-iron protein. It catalyzes a step in bacteriochlorophyll biosynthesis. |
| References | DR PFAM; PF00148; oxidored_nitro
RM 10811655
RT Reconstitution of light-independent protochlorophyllide reductase from purified bchl and BchN-BchB subunits. In vitro confirmation of nitrogenase-like features of a bacteriochlorophyll biosynthesis enzyme.
RA Fujita Y, Bauer CE
RL J Biol Chem 2000 Aug 4;275(31):23583-8
DR HAMAP; MF_00353; 84 of 104 |
| Genome Property | GenProp1004: light-independent protochlorophyllide reductase (HMM) |
