CYSH_SYNE7
ID CYSH_SYNE7 Reviewed; 232 AA.
AC Q55309; Q31K83; Q935X7;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2006, sequence version 2.
DT 03-AUG-2022, entry version 127.
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}; Synonyms=par;
GN OrderedLocusNames=Synpcc7942_2506; ORFNames=sea0019;
OS Synechococcus elongatus (strain PCC 7942 / FACHB-805) (Anacystis nidulans
OS R2).
OC Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae; Synechococcus.
OX NCBI_TaxID=1140;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1463852; DOI=10.1007/bf00028905;
RA Niehaus A., Gisselmann G., Schwenn J.D.;
RT "Primary structure of the Synechococcus PCC 7942 PAPS reductase gene.";
RL Plant Mol. Biol. 20:1179-1183(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Holtman C.K., Socias T., Mohler B.J., Chen Y., Min H., Golden S.S.,
RA Youderian P., Sandoval P., Gonzalez A., Salinas I.;
RT "Synechococcus elongatus PCC7942 genome sequence, cosmid 7H1 and 2E8.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7942 / FACHB-805;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA Hammon N., Israni S., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Kyrpides N., Lykidis A., Richardson P.;
RT "Complete sequence of chromosome 1 of Synechococcus elongatus PCC 7942.";
RL Submitted (AUG-2005) 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, ECO:0000305}.
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DR EMBL; M84476; AAA27328.1; -; Genomic_DNA.
DR EMBL; U30252; AAL03931.1; -; Genomic_DNA.
DR EMBL; CP000100; ABB58536.1; -; Genomic_DNA.
DR PIR; S28609; S28609.
DR RefSeq; WP_011243910.1; NC_007604.1.
DR AlphaFoldDB; Q55309; -.
DR SMR; Q55309; -.
DR STRING; 1140.Synpcc7942_2506; -.
DR PRIDE; Q55309; -.
DR EnsemblBacteria; ABB58536; ABB58536; Synpcc7942_2506.
DR KEGG; syf:Synpcc7942_2506; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_044089_3_0_3; -.
DR OMA; PIARWTQ; -.
DR OrthoDB; 674332at2; -.
DR BioCyc; SYNEL:SYNPCC7942_2506-MON; -.
DR UniPathway; UPA00140; UER00206.
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..232
FT /note="Phosphoadenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000100649"
FT ACT_SITE 228
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063"
FT CONFLICT 218
FT /note="S -> T (in Ref. 1; AAA27328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 232 AA; 26622 MW; 549FFECCB3BF89A6 CRC64;
MPALLPSLTE INAQLADQAA TQIIQWAATE FGSGLVLSTS FGIQSAVMLH LATQVQPDIP
VIWIDTGYLP TETYRFAAEL TERLKLNLKV YQSEISPARM EALYGRLWES ESVEDFNRYD
QMRKVEPMNR ALQELGATAW LSGVRRQQTA HRQSMEIVEL KRDRYAIRPI LGWHSRDVYQ
YLTAHDLPYH PLFDQGYVTV GDWHSSRPLQ ADDSDERSTR FRGLKQECGL HL
