InterPro : IPR002500

Name  Phosphoadenosine phosphosulphate reductase Short Name  PAPS_reduct
Type  Domain Description  This domain is found in phosphoadenosine phosphosulphate (PAPS) reductaseenzymes or PAPS sulphotransferase. PAPS reductase is part of the adenine nucleotide alpha hydrolases superfamily also including N type ATP PPasesand ATP sulphurylases []. The enzyme uses thioredoxin as an electron donor for the reduction of PAPS to phospho-adenosine-phosphate (PAP) [, ].It is also found in NodP nodulation protein P from Rhizobium meliloti(Sinorhizobium meliloti) which has ATPsulphurylase activity (sulphate adenylate transferase) [].

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

5 Found In

Id Name Short Name Type
IPR011784 Sulphate adenylyltransferase, small subunit SO4_adenylTrfase_ssu Family
IPR004508 Thioredoxin-independent 5'-adenylylsulphate reductase Thioredoxin-indep_APS_Rdtase Family
IPR011800 Phosphoadenosine phosphosulphate reductase CysH PAPS_reductase_CysH Family
IPR012183 FAD synthetase, molybdopterin binding FAD_synth_Mopterin-bd Family
IPR017598 Sulphur transferase DndC, putative SulphurTrfase_DndC_put Family

1 Parent Features

Id Name Short Name Type
IPR014729 Rossmann-like alpha/beta/alpha sandwich fold Rossmann-like_a/b/a_fold Domain

3 Publications

First Author Title Year Journal Volume Pages
Berendt U Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis. 1995 Eur J Biochem 233 347-56
Schwedock J ATP sulphurylase activity of the nodP and nodQ gene products of Rhizobium meliloti. 1990 Nature 348 644-7
Savage H Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases. 1997 Structure 5 895-906

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)