ID   CYSH_MYCBP              Reviewed;         254 AA.
AC   A1KL82;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   16-JUN-2009, entry version 19.
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=BCG_2406;
OS   Mycobacterium bovis (strain BCG / Pasteur 1173P2).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=410289;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17372194; DOI=10.1073/pnas.0700869104;
RA   Brosch R., Gordon S.V., Garnier T., Eiglmeier K., Frigui W.,
RA   Valenti P., Dos Santos S., Duthoy S., Lacroix C., Garcia-Pelayo C.,
RA   Inwald J.K., Golby P., Garcia J.N., Hewinson R.G., Behr M.A.,
RA   Quail M.A., Churcher C., Barrell B.G., Parkhill J., Cole S.T.;
RT   "Genome plasticity of BCG and impact on vaccine efficacy.";
RL   Proc. Natl. Acad. Sci. U.S.A. 104:5596-5601(2007).
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; AM408590; CAL72394.1; -; Genomic_DNA.
DR   RefSeq; YP_978495.1; -.
DR   GeneID; 4699205; -.
DR   GenomeReviews; AM408590_GR; BCG_2406.
DR   KEGG; mbb:BCG_2406; -.
DR   OMA; A1KL82; 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   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; 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_1000008929.
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
//