ID   CYSH_RHILO              Reviewed;         254 AA.
AC   Q98GP9;
DT   11-JUL-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   16-JUN-2009, entry version 42.
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=mll3228;
OS   Rhizobium loti (Mesorhizobium loti).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=381;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF303099;
RX   MEDLINE=21082930; PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA   Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA   Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T.,
RA   Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA   Mochizuki Y., Nakayama S., Nakazaki N., Shimpo S., Sugimoto M.,
RA   Takeuchi C., Yamada M., Tabata S.;
RT   "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT   Mesorhizobium loti.";
RL   DNA Res. 7:331-338(2000).
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; BA000012; BAB50167.1; -; Genomic_DNA.
DR   RefSeq; NP_104381.1; -.
DR   HSSP; P17854; 1SUR.
DR   GeneID; 1227042; -.
DR   GenomeReviews; BA000012_GR; mll3228.
DR   KEGG; mlo:mll3228; -.
DR   NMPDR; fig|266835.1.peg.2485; -.
DR   HOGENOM; Q98GP9; -.
DR   OMA; Q98GP9; FEETLAY.
DR   BRENDA; 1.8.4.8; 3315.
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    254       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_0000100639.
SQ   SEQUENCE   254 AA;  27605 MW;  F74E7CF045716CE3 CRC64;
     MLAKPRPLDH IGDADDGVAA KAAGLDALYG HLKPLEIIER SARELFHDEI AAVSSFGADS
     AVLLHMIAEI DRTLPVIFLD TGKHFEETLG YRDALVADFG LTNIQVIKPE EAALARIDPT
     GNLHQSNTDA CCDVRKVEPL ARGVAPFRAW FTGRKRFQAS TRAALPVFEA VGARIRINPL
     AHWTTSDQAD YMRAHALREN PLVAYGYLSI GCFPCTQPVQ PGEDARSGRW AGHAKTECGI
     HLSGLEVSLT DASL
//