ID   CYSH_STAS1              Reviewed;         242 AA.
AC   Q49UL7;
DT   22-NOV-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 33.
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=SSP2409;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 /
OS   DSM 20229).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K.,
RA   Higashide M., Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S.,
RA   Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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.
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DR   EMBL; AP008934; BAE19554.1; -; Genomic_DNA.
DR   RefSeq; YP_302499.1; -.
DR   GeneID; 3617313; -.
DR   GenomeReviews; AP008934_GR; SSP2409.
DR   KEGG; ssp:SSP2409; -.
DR   NMPDR; fig|342451.4.peg.2409; -.
DR   HOGENOM; Q49UL7; -.
DR   OMA; Q49UL7; GLATIDM.
DR   BioCyc; SSAP342451:SSP2409-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    242       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_0000100648.
SQ   SEQUENCE   242 AA;  27742 MW;  9179A05F32ACDAB5 CRC64;
     MSETKITYDD FNPHAFETLD ITDETKGARE VIRWAYDVYG DSIIYSCSFG AEGMILIDLI
     SSVKKDAEIV FLDTNLHFQE TYDLIDRVKA RYPELNIKLK QPSLTLEEQA DQVAPALWKQ
     DPNQCCYIRK IKPLEEVLSG ATAWVSGLRR EQSPSRQATN FINKDERFKS VKVCPLIHWT
     WDDVWDYIKA HDLHYNELHD FNFPSIGCIP CTEAVSGNGD SRAGRWTNST KTECGLHTTN
     KP
//