ID CYSH_VIBVU Reviewed; 258 AA. AC Q8CWK6; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 16-JUN-2009, entry version 43. 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=VV1_1404; OS Vibrio vulnificus. OC Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; OC Vibrionaceae; Vibrio. OX NCBI_TaxID=672; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CMCP6; RA Rhee J.H., Kim S.Y., Chung S.S., Kim J.J., Moon Y.H., Jeong H., RA Choy H.E.; RT "Complete genome sequence of Vibrio vulnificus CMCP6."; RL Submitted (DEC-2002) 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; AE016795; AAO09853.1; -; Genomic_DNA. DR RefSeq; NP_760326.1; -. DR HSSP; P17854; 1SUR. DR SMR; Q8CWK6; 7-235. DR GeneID; 1178325; -. DR GenomeReviews; AE016795_GR; VV1_1404. DR KEGG; vvu:VV1_1404; -. DR HOGENOM; Q8CWK6; -. DR OMA; Q8CWK6; TRFNGLK. DR BioCyc; VVUL216895:VV1_1404-MON; -. DR BRENDA; 1.8.4.8; 277169. 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 1 258 Phosphoadenosine phosphosulfate FT reductase. FT /FTId=PRO_0000100654. SQ SEQUENCE 258 AA; 29448 MW; C5078F647D681687 CRC64; MLDSVASTLQ LSELLSLTKA EQSIRLAEIN VELEMLSAQE RVAWALQNLE GAHAVSSSFG IQAAVMLHLV SKQQADIPVI LTDTGYLFPE TYQFIDELTK SLNLNLKVYR ANESANWQEA RYGKLWEQGI EGIEKYNKLN KVEPMRRALN ELNVKTWFSG LRREQSQSRA GLPILSIQNG VFKFLPVVDW SNKDVHYYLK EHGLSYHPLW EQGYLSVGDT HTTQKWEPGM SEEETRFFGL KRECGLHEED NEQDGSGI //