ID   CYSH_ALKEH              Reviewed;         245 AA.
AC   Q0A6T1;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 92.
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=Mlg_2114;
OS   Alkalilimnicola ehrlichii (strain ATCC BAA-1101 / DSM 17681 / MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1101 / DSM 17681 / MLHE-1;
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   Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Oremland R.S.,
RA   Hoeft S.E., Switzer-Blum J., Kulp T., King G., Tabita R., Witte B.,
RA   Santini J.M., Basu P., Hollibaugh J.T., Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) 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; CP000453; ABI57456.1; -; Genomic_DNA.
DR   RefSeq; WP_011629850.1; NC_008340.1.
DR   AlphaFoldDB; Q0A6T1; -.
DR   SMR; Q0A6T1; -.
DR   EnsemblBacteria; ABI57456; ABI57456; Mlg_2114.
DR   KEGG; aeh:Mlg_2114; -.
DR   eggNOG; COG0175; Bacteria.
DR   HOGENOM; CLU_044089_3_0_6; -.
DR   OMA; YNTEATY; -.
DR   OrthoDB; 674332at2; -.
DR   UniPathway; UPA00140; UER00206.
DR   Proteomes; UP000001962; 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; Reference proteome.
FT   CHAIN           1..245
FT                   /note="Phosphoadenosine 5'-phosphosulfate reductase"
FT                   /id="PRO_1000075068"
FT   ACT_SITE        239
FT                   /note="Nucleophile; cysteine thiosulfonate intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ   SEQUENCE   245 AA;  28176 MW;  0DFF948991CEED1C CRC64;
     MANRPQALKI HPQPVLAPGE LDSVRRQLAA ASAQERVRWG LARFPGRIVL ASSFGAQAAV
     SLHLVTREQP DIPVVLVDTG YLFPETYRFV DELTERLGLN LQVARPAHSA AWQEARFGRL
     WEQGVEGIER YNRMNKVEPM QQALETLGAD AWFAGLRRQQ AHSRQQRQVV EIQNDRVKVH
     PIIDWTDRDV HRYLTRHDLP YHPLWHEGYV SIGDVHTTRR LADGMSEEET RFFGLRRECG
     LHDLV