ID CYSH_ECOL5 Reviewed; 244 AA. AC Q0TEA4; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 05-SEP-2006, sequence version 1. DT 16-JUN-2009, entry version 24. 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=ECP_2736; OS Escherichia coli O6:K15:H31 (strain 536 / UPEC). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=362663; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16879640; DOI=10.1111/j.1365-2958.2006.05255.x; RA Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., RA Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.; RT "Role of pathogenicity island-associated integrases in the genome RT plasticity of uropathogenic Escherichia coli strain 536."; RL Mol. Microbiol. 61:584-595(2006). 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; CP000247; ABG70725.1; -; Genomic_DNA. DR RefSeq; YP_670626.1; -. DR SMR; Q0TEA4; 2-230. DR GeneID; 4191561; -. DR GenomeReviews; CP000247_GR; ECP_2736. DR KEGG; ecp:ECP_2736; -. DR HOGENOM; Q0TEA4; -. DR OMA; Q0TEA4; TRFNGLK. DR BioCyc; ECOL362663:ECP_2736-MON; -. 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; IPR004511; PAdo_PSO4_Rdtase_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 Complete proteome; Cytoplasm; Oxidoreductase. FT CHAIN 1 244 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_1000008922. SQ SEQUENCE 244 AA; 27975 MW; A7101CF0F0B6AC7D CRC64; MSKLDLNALN ELPKVDRILA LAETNAQLEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG //