| Accession | TIGR01281 |
| Name | DPOR_bchL |
| Function | light-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein |
| Gene Symbol | bchL |
| Trusted Cutoff | 345.15 |
| Domain Trusted Cutoff | 345.15 |
| Noise Cutoff | 280.45 |
| Domain Noise Cutoff | 280.45 |
| Isology Type | equivalog |
| EC Number | 1.18.-.- |
| HMM Length | 268 |
| 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 22 2001 8:49AM |
| Last Modified | Feb 14 2011 3:27PM |
| Comment | The BchL peptide (ChlL in chloroplast and cyanobacteria) is an ATP-binding iron-sulfur protein of the dark form protochlorophyllide reductase, an enzyme similar to nitrogenase. This subunit resembles the nitrogenase NifH subunit. |
| References | DR PFAM; PF00142; fer4_NifH
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_00355; 85 of 88 |
| Genome Property | GenProp1004: light-independent protochlorophyllide reductase (HMM) |
