CYSH_ECOLI
ID CYSH_ECOLI Reviewed; 244 AA.
AC P17854; Q2MA67;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Phosphoadenosine 5'-phosphosulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:17352498};
DE Short=PAPS reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:2404794};
DE EC=1.8.4.8 {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000269|PubMed:7588765};
DE AltName: Full=3'-phosphoadenylylsulfate reductase {ECO:0000255|HAMAP-Rule:MF_00063, ECO:0000303|PubMed:7588765};
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, ECO:0000303|PubMed:7588765};
GN Name=cysH {ECO:0000255|HAMAP-Rule:MF_00063};
GN OrderedLocusNames=b2762, JW2732;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2005873; DOI=10.1007/bf00269864;
RA Krone F.A., Westphal G., Schwenn J.D.;
RT "Characterisation of the gene cysH and of its product phospho-
RT adenylylsulphate reductase from Escherichia coli.";
RL Mol. Gen. Genet. 225:314-319(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B;
RX PubMed=2670946; DOI=10.1016/s0021-9258(19)84893-7;
RA Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M.,
RA Kredich N.M.;
RT "Characterization of the cysJIH regions of Salmonella typhimurium and
RT Escherichia coli B. DNA sequences of cysI and cysH and a model for the
RT siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on
RT amino acid homology with spinach nitrite reductase.";
RL J. Biol. Chem. 264:15726-15737(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP PROTEIN SEQUENCE OF 2-18.
RX PubMed=2404794; DOI=10.1016/0014-5793(90)80052-k;
RA Krone F.A., Westphal G., Meyer H.E., Schwenn J.D.;
RT "PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid
RT sequence with the DNA of gene cys H.";
RL FEBS Lett. 260:6-9(1990).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL
RP PROPERTIES, SUBUNIT, AND MUTAGENESIS OF TYR-209 AND CYS-239.
RX PubMed=7588765; DOI=10.1111/j.1432-1033.1995.347_1.x;
RA Berendt U., Haverkamp T., Prior A., Schwenn J.D.;
RT "Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase
RT investigated by site-directed mutagenesis.";
RL Eur. J. Biochem. 233:347-356(1995).
RN [7] {ECO:0007744|PDB:1SUR}
RP X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 2-216, SUBUNIT, AND DOMAIN.
RX PubMed=9261082; DOI=10.1016/s0969-2126(97)00244-x;
RA Savage H., Montoya G., Svensson C., Schwenn J.D., Sinning I.;
RT "Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new
RT family of adenine nucleotide alpha hydrolases.";
RL Structure 5:895-906(1997).
RN [8] {ECO:0007744|PDB:2O8V}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) IN COMPLEX WITH THIOREDOXIN,
RP SUBUNIT, AND ACTIVE SITE.
RX PubMed=17352498; DOI=10.1021/bi700130e;
RA Chartron J., Shiau C., Stout C.D., Carroll K.S.;
RT "3'-Phosphoadenosine-5'-phosphosulfate reductase in complex with
RT thioredoxin: a structural snapshot in the catalytic cycle.";
RL Biochemistry 46:3942-3951(2007).
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, ECO:0000269|PubMed:7588765}.
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 ECO:0000269|PubMed:7588765};
CC -!- ACTIVITY REGULATION: Severely inhibited by reagents which covalently
CC modify Cys groups in proteins. {ECO:0000269|PubMed:7588765}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for phosphoadenosine 5'-phosphosulfate
CC {ECO:0000269|PubMed:7588765};
CC KM=23 uM for thioredoxin {ECO:0000269|PubMed:7588765};
CC Vmax=94 umol/min/mg enzyme {ECO:0000269|PubMed:7588765};
CC -!- PATHWAY: Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from
CC sulfate: step 3/3. {ECO:0000255|HAMAP-Rule:MF_00063}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17352498,
CC ECO:0000269|PubMed:7588765, ECO:0000269|PubMed:9261082}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00063,
CC ECO:0000305}.
CC -!- DOMAIN: The open, reduced form of PAPS reductase is able to bind PAPS,
CC whereas the closed oxidized form cannot. A movement between the two
CC monomers of the dimer may allow this switch in conformation to occur.
CC {ECO:0000269|PubMed:9261082}.
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; Y07525; CAA68817.1; -; Genomic_DNA.
DR EMBL; M23008; AAA23652.1; -; Genomic_DNA.
DR EMBL; U29579; AAA69272.1; -; Genomic_DNA.
DR EMBL; U00096; AAC75804.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76839.1; -; Genomic_DNA.
DR PIR; S14221; RDECPA.
DR RefSeq; NP_417242.1; NC_000913.3.
DR RefSeq; WP_000039850.1; NZ_LN832404.1.
DR PDB; 1SUR; X-ray; 2.00 A; A=2-216.
DR PDB; 2O8V; X-ray; 3.00 A; A=1-244.
DR PDBsum; 1SUR; -.
DR PDBsum; 2O8V; -.
DR AlphaFoldDB; P17854; -.
DR SMR; P17854; -.
DR BioGRID; 4261451; 38.
DR IntAct; P17854; 4.
DR STRING; 511145.b2762; -.
DR jPOST; P17854; -.
DR PaxDb; P17854; -.
DR PRIDE; P17854; -.
DR EnsemblBacteria; AAC75804; AAC75804; b2762.
DR EnsemblBacteria; BAE76839; BAE76839; BAE76839.
DR GeneID; 947230; -.
DR KEGG; ecj:JW2732; -.
DR KEGG; eco:b2762; -.
DR PATRIC; fig|1411691.4.peg.3975; -.
DR EchoBASE; EB0186; -.
DR eggNOG; COG0175; Bacteria.
DR HOGENOM; CLU_044089_3_0_6; -.
DR InParanoid; P17854; -.
DR OMA; PIARWTQ; -.
DR PhylomeDB; P17854; -.
DR BioCyc; EcoCyc:PAPSSULFOTRANS-MON; -.
DR BioCyc; MetaCyc:PAPSSULFOTRANS-MON; -.
DR BRENDA; 1.8.4.8; 2026.
DR UniPathway; UPA00140; UER00206.
DR EvolutionaryTrace; P17854; -.
DR PRO; PR:P17854; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004604; F:phosphoadenylyl-sulfate reductase (thioredoxin) activity; IDA:EcoCyc.
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); IDA:EcoCyc.
DR GO; GO:0006790; P:sulfur compound metabolic process; IDA:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Oxidoreductase;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2404794"
FT CHAIN 2..244
FT /note="Phosphoadenosine 5'-phosphosulfate reductase"
FT /id="PRO_0000100630"
FT ACT_SITE 239
FT /note="Nucleophile; cysteine thiosulfonate intermediate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00063,
FT ECO:0000305|PubMed:17352498"
FT MUTAGEN 209
FT /note="Y->F: Strong decrease in activity. 400-fold decrease
FT in Vmax."
FT /evidence="ECO:0000269|PubMed:7588765"
FT MUTAGEN 239
FT /note="C->S: Almost inactive. 4500-fold decrease in Vmax.
FT Can still form dimers."
FT /evidence="ECO:0000269|PubMed:7588765"
FT CONFLICT 27
FT /note="E -> Q (in Ref. 2; AAA23652)"
FT /evidence="ECO:0000305"
FT CONFLICT 226
FT /note="A -> S (in Ref. 2; AAA23652)"
FT /evidence="ECO:0000305"
FT HELIX 6..10
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 14..28
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 33..43
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 46..51
FT /evidence="ECO:0007829|PDB:1SUR"
FT TURN 56..58
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 59..68
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 84..96
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 110..117
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 124..135
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 149..153
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:1SUR"
FT TURN 163..166
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 169..173
FT /evidence="ECO:0007829|PDB:1SUR"
FT STRAND 176..179
FT /evidence="ECO:0007829|PDB:1SUR"
FT TURN 181..184
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 187..197
FT /evidence="ECO:0007829|PDB:1SUR"
FT HELIX 203..207
FT /evidence="ECO:0007829|PDB:1SUR"
FT TURN 216..218
FT /evidence="ECO:0007829|PDB:2O8V"
SQ SEQUENCE 244 AA; 27976 MW; 7EC494ED2437E469 CRC64;
MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV
SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL
WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL
PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG
LHEG
