ID   CYSH_SALRD              Reviewed;         252 AA.
AC   Q2S5G4;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JAN-2006, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=SRU_0422;
OS   Salinibacter ruber (strain DSM 13855).
OC   Bacteria; Bacteroidetes; Sphingobacteria; Sphingobacteriales;
OC   Rhodothermaceae; Salinibacter.
OX   NCBI_TaxID=309807;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16330755; DOI=10.1073/pnas.0509073102;
RA   Mongodin E.F., Nelson K.E., Daugherty S., DeBoy R.T., Wister J.,
RA   Khouri H., Weidman J., Walsh D.A., Papke R.T., Sanchez Perez G.,
RA   Sharma A.K., Nesbo C.L., MacLeod D., Bapteste E., Doolittle W.F.,
RA   Charlebois R.L., Legault B., Rodriguez-Valera F.;
RT   "The genome of Salinibacter ruber: convergence and gene exchange among
RT   hyperhalophilic bacteria and archaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:18147-18152(2005).
CC   -!- FUNCTION: Reduction of activated sulfate into sulfite (By
CC       similarity).
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; CP000159; ABC44343.1; -; Genomic_DNA.
DR   RefSeq; YP_444567.1; -.
DR   GeneID; 3852402; -.
DR   GenomeReviews; CP000159_GR; SRU_0422.
DR   KEGG; sru:SRU_0422; -.
DR   NMPDR; fig|309807.5.peg.387; -.
DR   TIGR; SRU_0422; -.
DR   HOGENOM; Q2S5G4; -.
DR   OMA; Q2S5G4; FEETLAY.
DR   BioCyc; SRUB309807:SRU_0422-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: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; 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.
PE   3: Inferred from homology;
KW   Complete proteome; Cytoplasm; Oxidoreductase.
FT   CHAIN         1    252       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_1000075076.
SQ   SEQUENCE   252 AA;  28593 MW;  2007E8A7AB199D84 CRC64;
     MAFASDESAS PWSSTRLAAL NAQFEPHGPK AILNWATHTF GDDLAQGTGF GPSGIVIMHM
     LADLRPGTTV FYLDTDLLFP ETYELCDDLD ERLDVDVTRV HGGLSLDEQA EQEGEELWNR
     NPNRCCFLRK VKPLRNFLDD RRAWITGVRR DQSERRADTD ILSWEGQYGV FKINPLANWT
     QKEVWKYLFE HDLPYNPKHD QGYPSLGCVP CTEPVDQADG YSREGRWSDR DKTECGLHTS
     PEDEDGAHAA ES
//