CYSH_SALPK
ID CYSH_SALPK Reviewed; 244 AA.
AC B5BEZ7;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 68.
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=SSPA2611;
OS Salmonella paratyphi A (strain AKU_12601).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=554290;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AKU_12601;
RX PubMed=19159446; DOI=10.1186/1471-2164-10-36;
RA Holt K.E., Thomson N.R., Wain J., Langridge G.C., Hasan R., Bhutta Z.A.,
RA Quail M.A., Norbertczak H., Walker D., Simmonds M., White B., Bason N.,
RA Mungall K., Dougan G., Parkhill J.;
RT "Pseudogene accumulation in the evolutionary histories of Salmonella
RT enterica serovars Paratyphi A and Typhi.";
RL BMC Genomics 10:36-36(2009).
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; FM200053; CAR60852.1; -; Genomic_DNA.
DR RefSeq; WP_000080389.1; NC_011147.1.
DR AlphaFoldDB; B5BEZ7; -.
DR SMR; B5BEZ7; -.
DR KEGG; sek:SSPA2611; -.
DR HOGENOM; CLU_044089_3_0_6; -.
DR OMA; PIARWTQ; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000001869; 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_1000092185"
FT ACT_SITE 239
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ SEQUENCE 244 AA; 27952 MW; 1C9E07803478C18D CRC64;
MSQLDLNALN ELPKVDRVLA LAETNAQLET LTAEERVAWA LENLPGEYVL SSSFGIQAAV
SLHLVNQIRP DIPVILTDTG YLFPEAYQFI DELTDKLKLN LKVYRAGESP AWQEARYGKL
WEQGVEGIEK YNEINKVEPM NRALKELNAQ TWFAGLRREQ SGSRAHLPVL AIQRGVFKVL
PIIDWDNRTV YQYLQKHGLK YHPLWDQGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG
LHEG
