ID CYSH_BACSK Reviewed; 241 AA. AC Q5WKF5; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 23-NOV-2004, sequence version 1. DT 04-NOV-2008, entry version 29. 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; OrderedLocusNames=ABC0611; OS Bacillus clausii (strain KSM-K16). OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus. OX NCBI_TaxID=66692; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Takaki Y., Kageyama Y., Shimamura S., Suzuki H., Nishi S., Hatada Y., RA Kawai S., Ito S., Horikoshi K.; RT "The complete genome sequence of the alkaliphilic Bacillus clausii RT KSM-K16."; RL Submitted (OCT-2003) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Reduction of activated sulfate into sulfite (By CC similarity). 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; AP006627; BAD63150.1; -; Genomic_DNA. DR RefSeq; YP_174111.1; -. DR GeneID; 3204683; -. DR GenomeReviews; AP006627_GR; ABC0611. DR KEGG; bcl:ABC0611; -. DR NMPDR; fig|66692.3.peg.610; -. DR HOGENOM; Q5WKF5; -. DR BioCyc; BCLA66692:ABC0611-MON; -. DR GO; GO:0005737; C:cytoplasm; IEA:HAMAP. DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredo...; IEA:HAMAP. 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; IPR011798; APS_reductase. DR InterPro; IPR004511; CysH. DR InterPro; IPR002500; PAPS_reduct. 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; TIGR02055; APS_reductase; 1. DR TIGRFAMs; TIGR00434; cysH; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Oxidoreductase. FT CHAIN 1 241 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_1000075070. SQ SEQUENCE 241 AA; 28151 MW; 672C682B65E037A3 CRC64; MAYVFEQMEA TDYEKVNTKL KNRDSLDILR WANQTYGEKL VYACSFGAEA MVLLDLLSKI QKEAHILFLD TDFHFAETYE LIERVKERYP TFRINMAKPA LSPEEQAERY GDELWLKNPD QCCQIRKLDV LARELEPYDA WLSGLRREQS PTRANTEFVN QDKRFKKVKV CPLIHWTEEE IWMYIKLHQL PYNELHDQHY PSIGCTYCTK AVMPGEDARS GRWAGTGKTE CGLHAPTKGD S //