ID CYSH_SERP5 Reviewed; 244 AA. AC A8G9X8; DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot. DT 13-NOV-2007, sequence version 1. DT 16-JUN-2009, entry version 12. 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=Spro_0812; OS Serratia proteamaculans (strain 568). OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; OC Enterobacteriaceae; Serratia. OX NCBI_TaxID=399741; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., RA Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., RA Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., RA Kim E., Taghavi S., Newman L., Vangronsveld J., van der Lelie D., RA Richardson P.; RT "Complete sequence of chromosome of Serratia proteamaculans 568."; RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases. 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; CP000826; ABV39918.1; -; Genomic_DNA. DR RefSeq; YP_001477046.1; -. DR GeneID; 5603585; -. DR GenomeReviews; CP000826_GR; Spro_0812. DR KEGG; spe:Spro_0812; -. DR OMA; A8G9X8; TRFNGLK. 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_1000057433. SQ SEQUENCE 244 AA; 27755 MW; 43137392A5BB93CD CRC64; MAEFNLAELN ALPKSGQALS LAVVNGQLET LSAEQRVEWA LEHLPGEFVL SSSFGIQAAV CLHLVTRIKP DIPVILTDTG YLFPETYQFI DQLADKLKLN LQVFRAEQSP AWQEARYGKL WEQGVEGIEK YNQINKVEPM NRALETLGGQ TWFAGLRREQ SGSRAHLPVL AVQRGVFKIL PIIDWDNRKI YQYLTEHGLS YHPLWEQGYL SVGDTHTTQK WEPGMSEEET RFFGLKRECG LHEG //