ID CYSH_THIRO Reviewed; 239 AA. AC P52672; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 25-NOV-2008, entry version 51. DE RecName: Full=Phosphoadenosine phosphosulfate reductase; DE EC=1.8.4.8; DE AltName: Full=PAPS reductase, thioredoxin dependent; DE AltName: Full=PAdoPS reductase; DE AltName: Full=3'-phosphoadenylylsulfate reductase; DE AltName: Full=PAPS sulfotransferase; GN Name=cysH; OS Thiocapsa roseopersicina. OC Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales; OC Chromatiaceae; Thiocapsa. OX NCBI_TaxID=1058; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=DSM 219 / 6311; RX MEDLINE=96305328; PubMed=8695637; RA Bruehl A., Haverkamp T., Gisselmann G., Schwenn J.D.; RT "A cDNA clone from Arabidopsis thaliana encoding plastidic RT ferredoxin:sulfite reductase."; RL Biochim. Biophys. Acta 1295:119-124(1996). CC -!- FUNCTION: Reduction of activated sulfate into sulfite. CC -!- CATALYTIC ACTIVITY: Adenosine 3',5'-bisphosphate + sulfite + CC thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite CC from sulfate: step 3/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). CC -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Z23169; CAA80690.1; -; Genomic_DNA. DR PIR; S34193; S34193. DR HSSP; P17854; 1SUR. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredo...; IEA:HAMAP. DR GO; GO:0016740; F:transferase activity; IEA:InterPro. DR GO; GO:0019344; P:cysteine biosynthetic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. DR GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfa...; IEA:HAMAP. DR HAMAP; MF_00063; -; 1. DR InterPro; IPR004511; CysH. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR011800; PAPS_reductase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1. DR Pfam; PF01507; PAPS_reduct; 1. DR TIGRFAMs; TIGR00434; cysH; 1. DR TIGRFAMs; TIGR02057; PAPS_reductase; 1. PE 3: Inferred from homology; KW Cytoplasm; Oxidoreductase. FT CHAIN 1 239 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_0000100651. SQ SEQUENCE 239 AA; 27695 MW; 8677B99E6649255D CRC64; MSKPDLDAFL HGDDAALRET NRRLESMPAE DRVRWALEHL PPQHVLSSSF GTQSAVMLHL VSRQMPEIPV ILVDTGYLFP ETYRLVDALT DRFGLNLKVY RPALSPAWQE AGLGRLWEQG ADGIERYNRL NKIDPMERAL RDLDAGTWFA GLRRQQANSR AELPVLRRQD GRIKFHPIID WHRPRRARYL RRHDLPDHPL RDQGYVSIGD VHTTVPLLPG MLEEETRFFG IKRECGLHR //