|Domain Trusted Cutoff||165.10|
|Domain Noise Cutoff||95.95|
|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||Anolik RT, Haft DH|
|Entry Date||Apr 20 1999 2:07PM|
|Last Modified||Feb 14 2011 3:27PM|
|Comment||This enzyme, involved in the assimilation of inorganic sulfate, is designated cysH in Bacteria and MET16 in Saccharomyces cerevisiae. Synonyms include phosphoadenosine phosphosulfate reductase, PAPS reductase, and PAPS reductase, thioredoxin-dependent. In a reaction requiring reduced thioredoxin and NADPH, it converts 3(prime)-phosphoadenylylsulfate (PAPS) to sulfite and adenosine 3(prime),5(prime) diphosphate (PAP). A related family of plant enzymes, scoring below the trusted cutoff, differs in having a thioredoxin-like C-terminal domain, not requiring thioredoxin, and in having a preference for 5(prime)-adenylylsulfate (APS) over PAPS.|
RT Sulfate reduction in higher plants: molecular evidence for a novel 5'-adenylylsulfate reductase.
RA Setya A, Murillo M, Leustek T.
RL Proc Natl Acad Sci U S A. 1996 Nov 12;93(23):13383-8.
DR HAMAP; MF_00063; 86 of 92|
|Genome Property||GenProp0149: sulfate reduction to sulfide, assimilatory (HMM)|
© J. Craig Venter Institute | Privacy Statement | Data Disclaimer