ID   A3QAP1_SHELP            Unreviewed;       250 AA.
AC   A3QAP1;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   18-JUN-2025, entry version 115.
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=Shew_0667 {ECO:0000313|EMBL:ABO22539.1};
OS   Shewanella loihica (strain ATCC BAA-1088 / PV-4).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC   Alteromonadales; Shewanellaceae; Shewanella.
OX   NCBI_TaxID=323850 {ECO:0000313|EMBL:ABO22539.1, ECO:0000313|Proteomes:UP000001558};
RN   [1] {ECO:0000313|EMBL:ABO22539.1, ECO:0000313|Proteomes:UP000001558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1088 / PV-4 {ECO:0000313|Proteomes:UP000001558};
RG   US DOE Joint Genome Institute;
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., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Romine M.F., Serres G.,
RA   Fredrickson J., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella loihica PV-4.";
RL   Submitted (MAR-2007) 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: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; CP000606; ABO22539.1; -; Genomic_DNA.
DR   RefSeq; WP_011864473.1; NC_009092.1.
DR   AlphaFoldDB; A3QAP1; -.
DR   STRING; 323850.Shew_0667; -.
DR   KEGG; slo:Shew_0667; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_044089_3_0_6; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000001558; 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   GO; GO:0019379; P:sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin); IEA:UniProtKB-UniRule.
DR   CDD; cd23945; PAPS_reductase; 1.
DR   FunFam; 3.40.50.620:FF:000043; Phosphoadenosine phosphosulfate reductase; 1.
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; IPR011800; PAPS_reductase_CysH.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   NCBIfam; TIGR00434; cysH; 1.
DR   NCBIfam; TIGR02057; PAPS_reductase; 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|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00063};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW   Rule:MF_00063}; Reference proteome {ECO:0000313|Proteomes:UP000001558}.
FT   DOMAIN          53..225
FT                   /note="Phosphoadenosine phosphosulphate reductase"
FT                   /evidence="ECO:0000259|Pfam:PF01507"
FT   ACT_SITE        244
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   250 AA;  28389 MW;  FBD7D81D3CC92390 CRC64;
     MDNSVISAQA LQALLSAPKA EQDAELARVN AFLAGLTPAE RVIWGLAYLP GTHALSSSFG
     IQGAVMLHLV TQVQQDIPVI LTDTGYLFPE TYHFIDELTE RLKLNLKVYR APMTSAWQEA
     RFGRLWEQGL DGLEQYNRLN KVTPMQTALK ELEVGTWFAG LRRSQSSTRE DLPILAIHGD
     RYKLLPILEW SNKDVHEYLT KHDLPYHPLW EQGYVSVGDT HSSRPLELGM TEEETRFNGL
     KRECGLHYEI
//