ID CYSH_OCEIH Reviewed; 240 AA. AC Q8EQP2; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 39. 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=OB1652; OS Oceanobacillus iheyensis. OC Bacteria; Firmicutes; Bacillales; Bacillaceae; Oceanobacillus. OX NCBI_TaxID=182710; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 14371 / JCM 11309 / KCTC 3954 / HTE831; RX MEDLINE=22220767; PubMed=12235376; DOI=10.1093/nar/gkf526; RA Takami H., Takaki Y., Uchiyama I.; RT "Genome sequence of Oceanobacillus iheyensis isolated from the Iheya RT Ridge and its unexpected adaptive capabilities to extreme RT environments."; RL Nucleic Acids Res. 30:3927-3935(2002). 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; BA000028; BAC13608.1; -; Genomic_DNA. DR RefSeq; NP_692573.1; -. DR GeneID; 1018148; -. DR GenomeReviews; BA000028_GR; OB1652. DR KEGG; oih:OB1652; -. DR NMPDR; fig|221109.1.peg.1655; -. DR HOGENOM; Q8EQP2; -. DR OMA; Q8EQP2; FEETLAY. DR BioCyc; OIHE221109:OB1652-MON; -. DR BRENDA; 1.8.4.8; 278212. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. 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; IPR011798; APS_reductase. DR InterPro; IPR004511; PAdo_PSO4_Rdtase_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 1 240 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_1000008931. SQ SEQUENCE 240 AA; 27407 MW; 083D781AA9190CD9 CRC64; MGGYSVTYSN FVKDPYKDWF PDDETNGASK ILQWAYEVYG TDIVYACSFG AEGMVLIDLI SKTQKNADIV FLDTDLHFQE TYDLIEDIKV KYPTLNIHIK KPDLTLEEQA AEHGSALWKR QPDQCCYIRK IKPLEDALSG APAWISGLRR EQSVSRSKTD FINKDERFKS IKVCPLIHWT WDDVWEYIKD NNLPYNELHD NGYPSIGCIP CTSQVSDSSD SRAGRWAGTQ KTECGLHTSD //