ID   CYSH_ZYMMO              Reviewed;         244 AA.
AC   Q5NRM3;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   16-JUN-2009, entry version 32.
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=ZMO0007;
OS   Zymomonas mobilis.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Zymomonas.
OX   NCBI_TaxID=542;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 31821 / ZM4 / CP4;
RX   PubMed=15592456; DOI=10.1038/nbt1045;
RA   Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J.,
RA   Hong J.H., Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M.,
RA   Lee J.-S., Jin S.-J., Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y.,
RA   Kang H.L., Lee S.Y., Lee K.J., Kang H.S.;
RT   "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT   ZM4.";
RL   Nat. Biotechnol. 23:63-68(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.
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DR   EMBL; AE008692; AAV88631.1; -; Genomic_DNA.
DR   RefSeq; YP_161742.1; -.
DR   SMR; Q5NRM3; 2-230.
DR   GeneID; 3187620; -.
DR   GenomeReviews; AE008692_GR; ZMO0007.
DR   KEGG; zmo:ZMO0007; -.
DR   NMPDR; fig|264203.3.peg.503; -.
DR   HOGENOM; Q5NRM3; -.
DR   OMA; Q5NRM3; TRFNGLK.
DR   BioCyc; ZMOB264203:ZMO0007-MON; -.
DR   BRENDA; 1.8.4.8; 1658.
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_1000008949.
SQ   SEQUENCE   244 AA;  28262 MW;  B7D324FFF3D6B0C3 CRC64;
     MSAFHLETLK SLPKAEQEAA LSEANRQLEE MSAEDRLKWA FDNLSGQFVL SSSFGIQAAV
     MLHLVTRKKA DIPVILTDTG YLFPETYRFI DALTEKLDLN LQVFRAALSP AWQEARYGKL
     WEQGVEGIER YNDINKVEPM NRALKTLEAG TWFAGLRRDQ SKSRSHLPIL AIQRGVFKFL
     PIIDWDNRKI HYYLKEHDLP YHPLWDEGYL SVGDTHTTRK WEEGMSEEET RFFGLKRECG
     LHEG
//