ID   CYSH_BACCR              Reviewed;         234 AA.
AC   Q81FZ1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   16-JUN-2009, entry version 41.
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=BC_1421;
OS   Bacillus cereus (strain ATCC 14579 / DSM 31).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=226900;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22608415; PubMed=12721630; DOI=10.1038/nature01582;
RA   Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B.,
RA   Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A.,
RA   Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T.,
RA   Grechkin Y., Pusch G., Haselkorn R., Fonstein M., Ehrlich S.D.,
RA   Overbeek R., Kyrpides N.C.;
RT   "Genome sequence of Bacillus cereus and comparative analysis with
RT   Bacillus anthracis.";
RL   Nature 423:87-91(2003).
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; AE016877; AAP08402.1; -; Genomic_DNA.
DR   RefSeq; NP_831201.1; -.
DR   HSSP; P17854; 1SUR.
DR   GeneID; 1203770; -.
DR   GenomeReviews; AE016877_GR; BC_1421.
DR   KEGG; bce:BC1421; -.
DR   HOGENOM; Q81FZ1; -.
DR   OMA; Q81FZ1; TRFNGLK.
DR   BioCyc; BCER226900:BC_1421-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; 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    234       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_0000100624.
SQ   SEQUENCE   234 AA;  27342 MW;  DF04BC7D391D8B77 CRC64;
     MLTYETWEEN VVSFSEEDET KGALSVLNWA YKEYKDEVVY ACSFGVEGMV LLHIINQVNP
     SAKVVFLDTN VHFQETYELI RKVRERFPSL NIIEKQPELT LDEQAKLHGE KLWESNPNLC
     CKIRKILPLE KSLVVEKAWI SGLRREQSET RKHTKFINQD HRFQSIKVCP LIHWTWKEVW
     RYVYKHSLPY NPLHDVGYPS IGCEKCTLPV GDGGDSRDGR WAGKVKTECG LHYQ
//