Accession | TIGR02057 |
Name | PAPS_reductase |
Function | phosphoadenosine phosphosulfate reductase |
Gene Symbol | cysH |
Trusted Cutoff | 254.20 |
Domain Trusted Cutoff | 254.20 |
Noise Cutoff | 228.85 |
Domain Noise Cutoff | 228.85 |
Isology Type | equivalog |
EC Number | 1.8.4.8 |
HMM Length | 224 |
Mainrole Category | Central intermediary metabolism |
Subrole Category | Sulfur metabolism |
Gene Ontology Term | GO:0004604: phosphoadenylyl-sulfate reductase (thioredoxin) activity molecular_function |
| GO:0019379: sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) biological_process |
Author | Brinkac L |
Entry Date | Nov 11 2003 3:59PM |
Last Modified | Feb 14 2011 3:27PM |
Comment | Requiring thioredoxin as an electron donor, phosphoadenosine phosphosulfate reductase catalyzes the reduction of 3'-phosphoadenylylsulfate (PAPS) to sulfite and phospho-adenosine-phosphate (PAP). Found in enterobacteria, cyanobacteria, and yeast, PAPS reductase is related to a group of plant (TIGR00424) and bacterial (TIGR02055) enzymes preferring 5'-adenylylsulfate (APS) over PAPS as a substrate for reduction to sulfite [2]. |
References | RN [1]
RM 9261082
RT Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.
RA Savage H, Montoya G, Svensson C, Schwenn JD, Sinning I.
RL Structure. 1997 Jul 15;5(7):895-906.
RN [2]
RM 10613872
RT Identification of a new class of 5'-adenylylsulfate (APS) reductases from sulfate-assimilating bacteria.
RA Bick JA, Dennis JJ, Zylstra GJ, Nowack J, Leustek T.
RT J Bacteriol. 2000 Jan;182(1):135-42.
DR PFAM; PF01507; Phosphoadenosine phosphosulfate reductase family
DR EXPERIMENTAL; SP|P17854; Escherichia coli; crystal structure determined to 2.0A resolution; catalytic properties measured.
DR EXPERIMENTAL; SP|P18408; Saccharomyces cerevisiae; site-directed mutagenesis.
DR HAMAP; MF_00063; 54 of 92 |
Genome Property | GenProp0149: sulfate reduction to sulfide, assimilatory (HMM) |