ID   CYSH_SHISS              Reviewed;         244 AA.
AC   Q3YY96;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=SSON_2915;
OS   Shigella sonnei (strain Ss046).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Shigella.
OX   NCBI_TaxID=300269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16275786; DOI=10.1093/nar/gki954;
RA   Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X.,
RA   Wang J., Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S.,
RA   Nie H., Peng J., Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y.,
RA   Qiang B., Hou Y., Yu J., Jin Q.;
RT   "Genome dynamics and diversity of Shigella species, the etiologic
RT   agents of bacillary dysentery.";
RL   Nucleic Acids Res. 33:6445-6458(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.
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; CP000038; AAZ89516.1; -; Genomic_DNA.
DR   RefSeq; YP_311751.1; -.
DR   SMR; Q3YY96; 2-230.
DR   GeneID; 3667692; -.
DR   GenomeReviews; CP000038_GR; SSON_2915.
DR   KEGG; ssn:SSON_2915; -.
DR   HOGENOM; Q3YY96; -.
DR   OMA; Q3YY96; TRFNGLK.
DR   BioCyc; SSON300269:SSO_2915-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: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_1000008939.
SQ   SEQUENCE   244 AA;  27992 MW;  7EC48AECC437E469 CRC64;
     MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV
     SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL
     WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL
     PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMSEEET RFFGLKRECG
     LHEG
//