HMM Summary Page: TIGR02057

Functionphosphoadenosine phosphosulfate reductase
Gene SymbolcysH
Trusted Cutoff254.20
Domain Trusted Cutoff254.20
Noise Cutoff228.85
Domain Noise Cutoff228.85
Isology Typeequivalog
EC Number1.8.4.8
HMM Length224
Mainrole CategoryCentral intermediary metabolism
Subrole CategorySulfur metabolism
Gene Ontology TermGO:0004604: phosphoadenylyl-sulfate reductase (thioredoxin) activity molecular_function
GO:0019379: sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) biological_process
AuthorBrinkac L
Entry DateNov 11 2003 3:59PM
Last ModifiedFeb 14 2011 3:27PM
CommentRequiring 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].
ReferencesRN [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 PropertyGenProp0149: sulfate reduction to sulfide, assimilatory (HMM)