Accession | TIGR00424 |
Name | APS_reduc |
Function | 5'-adenylylsulfate reductase, thioredoxin-independent |
Trusted Cutoff | 553.20 |
Domain Trusted Cutoff | 553.20 |
Noise Cutoff | 347.35 |
Domain Noise Cutoff | 347.35 |
Isology Type | equivalog |
HMM Length | 464 |
Mainrole Category | Central intermediary metabolism |
Subrole Category | Sulfur metabolism |
Gene Ontology Term | GO:0006790: sulfur compound metabolic process biological_process |
| GO:0016667: oxidoreductase activity, acting on a sulfur group of donors molecular_function |
Author | Haft DH |
Entry Date | Apr 20 1999 2:03PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | This enzyme, involved in the assimilation of inorganic sulfate, is closely related to the thioredoxin-dependent PAPS reductase of Bacteria (CysH) and Saccharomyces cerevisiae. However, it has its own C-terminal thioredoxin-like domain and is not thioredoxin-dependent. Also, it has a substrate preference for 5'-adenylylsulfate (APS) over 3'-phosphoadenylylsulfate (PAPS) so the pathway does not require an APS kinase (CysC) to convert APS to PAPS. Arabidopsis thaliana appears to have three isozymes, all able to complement E. coli CysH mutants (even in backgrounds lacking thioredoxin or APS kinase) but likely localized to different compartments in Arabidopsis. |
References | RM 97075174
SE TIGR
GA hmmls |