| Accession | TIGR00434 |
| Name | cysH |
| Function | phosophoadenylyl-sulfate reductase |
| Gene Symbol | cysH |
| Trusted Cutoff | 165.10 |
| Domain Trusted Cutoff | 165.10 |
| Noise Cutoff | 95.95 |
| Domain Noise Cutoff | 95.95 |
| Isology Type | subfamily |
| EC Number | 1.8.4.8 |
| HMM Length | 214 |
| 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. |
| References | SE TIGR
RN [1]
RM 8917600
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) |
