ID CYSH_MYCTA Reviewed; 254 AA. AC A5U586; DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot. DT 10-JUL-2007, sequence version 1. DT 16-JUN-2009, entry version 16. 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=MRA_2416; OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra). OC Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales; OC Corynebacterineae; Mycobacteriaceae; Mycobacterium; OC Mycobacterium tuberculosis complex. OX NCBI_TaxID=419947; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Wang S.Y., Zheng H.J., Lv L.D., Wang B.F., Zhang X.L., Pu S.Y., RA Zhu G.F., Wang H.H., Zhao G.P., Zhang Y.; RT "Complete genomic sequence of Mycobacterium tuberculosis strain H37Ra, RT a non-pathogenic variant closely related to the well-characterized RT pathogenic strain H37Rv."; RL Submitted (MAR-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; CP000611; ABQ74186.1; -; Genomic_DNA. DR RefSeq; YP_001283748.1; -. DR GeneID; 5213172; -. DR GenomeReviews; CP000611_GR; MRA_2416. DR KEGG; mra:MRA_2416; -. DR OMA; A5U586; FEETLAY. 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 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 1 254 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_1000008930. SQ SEQUENCE 254 AA; 27423 MW; 554F2E3204452C55 CRC64; MSGETTRLTE PQLRELAARG AAELDGATAT DMLRWTDETF GDIGGAGGGV SGHRGWTTCN YVVASNMADA VLVDLAAKVR PGVPVIFLDT GYHFVETIGT RDAIESVYDV RVLNVTPEHT VAEQDELLGK DLFARNPHEC CRLRKVVPLG KTLRGYSAWV TGLRRVDAPT RANAPLVSFD ETFKLVKVNP LAAWTDQDVQ EYIADNDVLV NPLVREGYPS IGCAPCTAKP AEGADPRSGR WQGLAKTECG LHAS //