HMM Summary Page: TIGR01281

Functionlight-independent protochlorophyllide reductase, iron-sulfur ATP-binding protein
Gene SymbolbchL
Trusted Cutoff345.15
Domain Trusted Cutoff345.15
Noise Cutoff280.45
Domain Noise Cutoff280.45
Isology Typeequivalog
EC Number1.3.7.7
HMM Length268
Mainrole CategoryBiosynthesis of cofactors, prosthetic groups, and carriers
Subrole CategoryChlorophyll and bacteriochlorphyll
Gene Ontology TermGO:0015995: chlorophyll biosynthetic process biological_process
GO:0016491: oxidoreductase activity molecular_function
AuthorHaft DH
Entry DateJun 22 2001 8:49AM
Last ModifiedFeb 14 2011 3:27PM
CommentThe 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.
ReferencesDR 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 PropertyGenProp1004: light-independent protochlorophyllide reductase (HMM)