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UniProtKB/Swiss-Prot entry P17854


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name CYSH_ECOLI
Primary accession number P17854
Secondary accession number Q2MA67
Integrated into Swiss-Prot on November 1, 1990
Sequence was last modified on January 23, 2007 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 82)
Name and origin of the protein
Protein name Phosphoadenosine phosphosulfate reductase
Synonyms EC 1.8.4.8
PAPS reductase, thioredoxin dependent
PAdoPS reductase
3'-phosphoadenylylsulfate reductase
PAPS sulfotransferase
Gene name
Name: cysH
OrderedLocusNames: b2762, JW2732
From
Escherichia coli (strain K12) [TaxID: 83333] [HAMAP proteome]
Taxonomy Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales; Enterobacteriaceae; Escherichia.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=K12;
DOI=10.1007/BF00269864; PubMed=2005873 [NCBI, ExPASy, EBI, Israel, Japan]
Krone F.A., Westphal G., Schwenn J.D.;
"Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli.";
Mol. Gen. Genet. 225:314-319(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
STRAIN=B;
PubMed=2670946 [NCBI, ExPASy, EBI, Israel, Japan]
Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M.;
"Characterization of the cysJIH regions of Salmonella typhimurium and Escherichia coli B. DNA sequences of cysI and cysH and a model for the siroheme-Fe4S4 active center of sulfite reductase hemoprotein based on amino acid homology with spinach nitrite reductase.";
J. Biol. Chem. 264:15726-15737(1989).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
DOI=10.1126/science.277.5331.1453; PubMed=9278503 [NCBI, ExPASy, EBI, Israel, Japan]
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1474(1997).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
DOI=10.1038/msb4100049; PubMed=16738553 [NCBI, ExPASy, EBI, Israel, Japan]
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[5]
PROTEIN SEQUENCE OF 2-18.
DOI=10.1016/0014-5793(90)80052-K; PubMed=2404794 [NCBI, ExPASy, EBI, Israel, Japan]
Krone F.A., Westphal G., Meyer H.E., Schwenn J.D.;
"PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H.";
FEBS Lett. 260:6-9(1990).
[6]
CHARACTERIZATION, AND MUTAGENESIS.
PubMed=7588765 [NCBI, ExPASy, EBI, Israel, Japan]
Berendt U., Haverkamp T., Prior A., Schwenn J.D.;
"Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis.";
Eur. J. Biochem. 233:347-356(1995).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
DOI=10.1016/S0969-2126(97)00244-X; PubMed=9261082 [NCBI, ExPASy, EBI, Israel, Japan]
Savage H., Montoya G., Svensson C., Schwenn J.D., Sinning I.;
"Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases.";
Structure 5:895-906(1997).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
Y07525; CAA68817.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M23008; AAA23652.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U29579; AAA69272.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U00096; AAC75804.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AP009048; BAE76839.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR S14221; RDECPA.
RefSeq AP_003329.1; -.
NP_417242.1; -.
3D structure databases
PDB
1SUR; X-ray; 2.00 A; A=1-216.[ExPASy / RCSB / EBI]
2O8V; X-ray; 3.00 A; A=1-244.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1SUR; -.
2O8V; -.
ModBase P17854.
Protein-protein interaction databases
IntAct P17854; -.
Enzyme and pathway databases
BioCyc EcoCyc:PAPSSULFOTRANS-MON; -.
Organism-specific databases
EchoBASE EB0186; -.
EcoGene EG10189; cysH.
Ontologies
GO
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
QuickGo view.
Family and domain databases
HAMAP MF_00063; -; 1.
PBIL [Tree]
InterPro IPR004511; CysH.
IPR002500; PAPS_reduct.
IPR011800; PAPS_reductase.
IPR014729; Rossmann-like_a/b/a_fold.
Graphical view of domain structure.
Gene3D G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
Pfam PF01507; PAPS_reduct; 1.
Pfam graphical view of domain structure.
TIGRFAMs TIGR00434; cysH; 1.
TIGR02057; PAPS_reductase; 1.
BLOCKS P17854.
Genome annotation databases
GeneID 947230; -.
GenomeReviews U00096_GR; b2762.
AP009048_GR; JW2732.
KEGG ecj:JW2732; -.
eco:b2762; -.
Phylogenomic databases
HOGENOM P17854; -.
Genome annotation databases
CMR P17854; b2762.
Other
ProtoNet P17854.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; Oxidoreductase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   244  243     Phosphoadenosine phosphosulfate reductase. PRO_0000100630
MUTAGEN   209   209        Y->F: Reduction in Vmax. 
MUTAGEN   239   239        C->S: 5-fold reduction in Vmax. 
CONFLICT   27    27        E -> Q (in Ref. 2; AAA23652). 
CONFLICT   226   226        A -> S (in Ref. 2; AAA23652). 
HELIX   6    10  5      
HELIX   14    28  15      
HELIX   33    43  11      
STRAND   46    51  6      
TURN   56    58  3      
HELIX   59    68  10      
STRAND   73    78  6      
HELIX   84    96  13      
STRAND   100   105  6      
HELIX   110   117  8      
HELIX   120   122  3      
HELIX   124   135  12      
HELIX   137   146  10      
STRAND   149   153  5      
STRAND   160   162  3      
TURN   163   166  4      
STRAND   169   173  5      
STRAND   176   179  4      
TURN   181   184  4      
HELIX   187   197  11      
HELIX   203   207  5      
Sequence information
Length: 244 AA [This is the length of the unprocessed precursor] Molecular weight: 27976 Da [This is the MW of the unprocessed precursor] CRC64: 7EC494ED2437E469 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL SSSFGIQAAV 

        70         80         90        100        110        120 
SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN LKVYRATESA AWQEARYGKL 

       130        140        150        160        170        180 
WEQGVEGIEK YNDINKVEPM NRALKELNAQ TWFAGLRREQ SGSRANLPVL AIQRGVFKVL 

       190        200        210        220        230        240 
PIIDWDNRTI YQYLQKHGLK YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG 


LHEG 

P17854 in FASTA format

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