CYSH_BUCAI
ID CYSH_BUCAI Reviewed; 244 AA.
AC P57501;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 1.
DT 25-MAY-2022, entry version 116.
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=BU426;
OS Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS pisum symbiotic bacterium).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Buchnera.
OX NCBI_TaxID=107806;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=APS;
RX PubMed=10993077; DOI=10.1038/35024074;
RA Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT sp. APS.";
RL Nature 407:81-86(2000).
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, ECO:0000305}.
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DR EMBL; BA000003; BAB13124.1; -; Genomic_DNA.
DR RefSeq; NP_240238.1; NC_002528.1.
DR RefSeq; WP_010896110.1; NC_002528.1.
DR AlphaFoldDB; P57501; -.
DR SMR; P57501; -.
DR STRING; 107806.10039090; -.
DR EnsemblBacteria; BAB13124; BAB13124; BAB13124.
DR KEGG; buc:BU426; -.
DR PATRIC; fig|107806.10.peg.435; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_044089_3_0_6; -.
DR OMA; PIARWTQ; -.
DR UniPathway; UPA00140; UER00206.
DR Proteomes; UP000001806; 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..244
FT /note="Phosphoadenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000100628"
FT ACT_SITE 239
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
SQ SEQUENCE 244 AA; 28402 MW; ED7ADB9778927DDB CRC64;
MSKFYIENIN LLNSEKKNNI LSELNLLLSN YSAEERISWA LSHLPHTQIM SSSFGIQSTV
LLHLIIKKKP DIPVILIDTG YLFPETYNFI DFLTNKFHLN LKVFRSTISS AWQEARYGKL
WEKGIEGIDF YNNINKVQPM NFALNELSVQ TWFAGLRHDQ SKSRNLLPYL SIKKGIFKIL
PILDWSKDKI KDYLKENNLD THPLYNNGYS SVGDTHTTKK HMPGMLEEET RFFGLKRECG
LHEN
