ID   A9WRR2_RENSM            Unreviewed;       187 AA.
AC   A9WRR2;
DT   05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT   05-FEB-2008, sequence version 1.
DT   04-NOV-2026, entry version 82.
DE   RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            Short=PAPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE            EC=1.8.4.8 {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS reductase, thioredoxin dependent {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAPS sulfotransferase {ECO:0000256|HAMAP-Rule:MF_00063};
DE   AltName: Full=PAdoPS reductase {ECO:0000256|HAMAP-Rule:MF_00063};
GN   Name=cysH {ECO:0000256|HAMAP-Rule:MF_00063};
GN   OrderedLocusNames=RSal33209_2619 {ECO:0000313|EMBL:ABY24344.1};
OS   Renibacterium salmoninarum (strain ATCC 33209 / DSM 20767 / JCM 11484 /
OS   NBRC 15589 / NCIMB 2235).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Micrococcaceae; Renibacterium.
OX   NCBI_TaxID=288705 {ECO:0000313|EMBL:ABY24344.1, ECO:0000313|Proteomes:UP000002007};
RN   [1] {ECO:0000313|Proteomes:UP000002007}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33209 / DSM 20767 / JCM 11484 / NBRC 15589 / NCIMB 2235
RC   {ECO:0000313|Proteomes:UP000002007};
RX   PubMed=18723615; DOI=10.1128/JB.00721-08;
RA   Wiens G.D., Rockey D.D., Wu Z., Chang J., Levy R., Crane S., Chen D.S.,
RA   Capri G.R., Burnett J.R., Sudheesh P.S., Schipma M.J., Burd H.,
RA   Bhattacharyya A., Rhodes L.D., Kaul R., Strom M.S.;
RT   "Genome sequence of the fish pathogen Renibacterium salmoninarum suggests
RT   reductive evolution away from an environmental Arthrobacter ancestor.";
RL   J. Bacteriol. 190:6970-6982(2008).
CC   -!- FUNCTION: Catalyzes the formation of sulfite from phosphoadenosine 5'-
CC       phosphosulfate (PAPS) using thioredoxin as an electron donor.
CC       {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[thioredoxin]-disulfide + sulfite + adenosine 3',5'-
CC         bisphosphate + 2 H(+) = [thioredoxin]-dithiol + 3'-phosphoadenylyl
CC         sulfate; Xref=Rhea:RHEA:11724, Rhea:RHEA-COMP:10698, Rhea:RHEA-
CC         COMP:10700, 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:0000256|HAMAP-Rule:MF_00063};
CC   -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC       sulfate: step 3/3. {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- SIMILARITY: Belongs to the PAPS reductase family. CysH subfamily.
CC       {ECO:0000256|ARBA:ARBA00009732, ECO:0000256|HAMAP-Rule:MF_00063}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00063}.
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DR   EMBL; CP000910; ABY24344.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9WRR2; -.
DR   STRING; 288705.RSal33209_2619; -.
DR   KEGG; rsa:RSal33209_2619; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_044089_2_0_11; -.
DR   OMA; AACCQMR; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000002007; 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-UniRule.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   HAMAP; MF_00063; CysH; 1.
DR   InterPro; IPR004511; PAPS/APS_Rdtase.
DR   InterPro; IPR002500; PAPS_reduct_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 1.
DR   NCBIfam; NF002537; PRK02090.1; 1.
DR   PANTHER; PTHR46509; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   PANTHER; PTHR46509:SF1; PHOSPHOADENOSINE PHOSPHOSULFATE REDUCTASE; 1.
DR   Pfam; PF01507; PAPS_reduct; 1.
DR   PIRSF; PIRSF000857; PAPS_reductase; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00063}; Reference proteome {ECO:0000313|Proteomes:UP000002007}.
FT   DOMAIN          3..163
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   ACT_SITE        183
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   187 AA;  20845 MW;  46278EE5AC117DC2 CRC64;
     MADAVLPALV ADQLPDVDVL FLETGYHFPE THDTRREVAE NLRVNIVDVL PEQTIAQQEV
     ARGKDLFARN PAQYCQLRKM DPLKKALSGY EVWFTGVRRD EAPTRTNTPL VTWDEAHGLV
     KVNPMAAWSL DALVSYTEEH IIPVNPLMSR GFLSIGCVPC TRPVAVGEDP RAGHWAGFDK
     TECGIHI
//