ID   CYSH_ECOLC              Reviewed;         244 AA.
AC   B1IUR7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 74.
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=EcolC_0950;
OS   Escherichia coli (strain ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 /
OS   WDCM 00012 / Crooks).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=481805;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8739 / DSM 1576 / NBRC 3972 / NCIMB 8545 / WDCM 00012 / Crooks;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Ingram L., Richardson P.;
RT   "Complete sequence of Escherichia coli C str. ATCC 8739.";
RL   Submitted (FEB-2008) to the EMBL/GenBank/DDBJ databases.
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; CP000946; ACA76619.1; -; Genomic_DNA.
DR   RefSeq; WP_000039850.1; NZ_CP022959.1.
DR   AlphaFoldDB; B1IUR7; -.
DR   SMR; B1IUR7; -.
DR   KEGG; ecl:EcolC_0950; -.
DR   HOGENOM; CLU_044089_3_0_6; -.
DR   OMA; PIARWTQ; -.
DR   UniPathway; UPA00140; UER00206.
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_1000075071"
FT   ACT_SITE        239
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   244 AA;  27976 MW;  7EC494ED2437E469 CRC64;
     MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV
     SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL
     WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL
     PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG
     LHEG