ID   CYSH_ALHEH              Reviewed;         245 AA.
AC   Q0A6T1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
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=Mlg_2114;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Reduction of activated sulfate into sulfite (By
CC       similarity).
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; CP000453; ABI57456.1; -; Genomic_DNA.
DR   RefSeq; YP_742946.1; -.
DR   GeneID; 4269364; -.
DR   GenomeReviews; CP000453_GR; Mlg_2114.
DR   KEGG; aeh:Mlg_2114; -.
DR   HOGENOM; Q0A6T1; -.
DR   OMA; Q0A6T1; AWTDEDM.
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    245       Phosphoadenosine phosphosulfate
FT                                reductase.
FT                                /FTId=PRO_1000075068.
SQ   SEQUENCE   245 AA;  28176 MW;  0DFF948991CEED1C CRC64;
     MANRPQALKI HPQPVLAPGE LDSVRRQLAA ASAQERVRWG LARFPGRIVL ASSFGAQAAV
     SLHLVTREQP DIPVVLVDTG YLFPETYRFV DELTERLGLN LQVARPAHSA AWQEARFGRL
     WEQGVEGIER YNRMNKVEPM QQALETLGAD AWFAGLRRQQ AHSRQQRQVV EIQNDRVKVH
     PIIDWTDRDV HRYLTRHDLP YHPLWHEGYV SIGDVHTTRR LADGMSEEET RFFGLRRECG
     LHDLV
//