ID   CYSH_YERE8              Reviewed;         244 AA.
AC   A1JJS4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 83.
DE   RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE            Short=PAPS reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.8 {ECO:0000255|HAMAP-Rule:MF_00063};
DE   AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000255|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS sulfotransferase {ECO:0000255|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAdoPS reductase {ECO:0000255|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000255|HAMAP-Rule:MF_00063}; OrderedLocusNames=YE0757;
OS   Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS   8081).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=393305;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 13174 / 8081;
RX   PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA   Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA   Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA   Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA   Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA   Prentice M.B.;
RT   "The complete genome sequence and comparative genome analysis of the high
RT   pathogenicity Yersinia enterocolitica strain 8081.";
RL   PLoS Genet. 2:2039-2051(2006).
CC   -!- FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'-
CC       phosphosulfate (PAPS) using thioredoxin as an electron donor.
CC       {ECO:0000255|HAMAP-Rule:MF_00063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + adenosine 3',5'-bisphosphate + 2
CC         H(+) + sulfite = 3'-phosphoadenylyl sulfate + [thioredoxin]-dithiol;
CC         Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-COMP:10700,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:17359, ChEBI:CHEBI:29950,
CC         ChEBI:CHEBI:50058, ChEBI:CHEBI:58339, ChEBI:CHEBI:58343; EC=1.8.4.8;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00063};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_00063}.
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DR   EMBL; AM286415; CAL10861.1; -; Genomic_DNA.
DR   RefSeq; WP_005167272.1; NC_008800.1.
DR   RefSeq; YP_001005101.1; NC_008800.1.
DR   AlphaFoldDB; A1JJS4; -.
DR   SMR; A1JJS4; -.
DR   STRING; 393305.YE0757; -.
DR   EnsemblBacteria; CAL10861; CAL10861; YE0757.
DR   KEGG; yen:YE0757; -.
DR   PATRIC; fig|393305.7.peg.851; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_044089_3_0_6; -.
DR   OMA; PIARWTQ; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000000642; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0070814; P:hydrogen sulfide biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-UniRule.
DR   CDD; cd01713; PAPS_reductase; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct.
DR   InterPro; IPR011800; PAPS_reductase_CysH.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   TIGRFAMs; TIGR00434; cysH; 1.
DR   TIGRFAMs; TIGR02057; PAPS_reductase; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Oxidoreductase.
FT   CHAIN           1..244
FT                   /note="Phosphoadenosine 5'-phosphosulfate reductase"
FT                   /id="PRO_1000008947"
FT   ACT_SITE        239
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   244 AA;  27847 MW;  993D0E68A366A675 CRC64;
     MSQFNLNELN ALPKAEQAAA LALVNGQLEH LTAQERVSWA LENLPGEFVL SSSFGIQAAV
     CLHLVTRQQP DIPVILTDTG YLFPETYQFI DSLTEKLQLN LQVFRAQQSP AWQEARYGKL
     WEQGVEGIER YNDLNKVEPM NRALETLGAQ TWFAGLRREQ SGSRAKLPVL AIARGVFKLL
     PIIDWDNRQV YQYLTQHGLS YHPLWEQGYL SVGDTHTTRK WEPGMSEEET RFFGLKRECG
     LHES