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P17854 (CYSH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 129. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Phosphoadenosine phosphosulfate reductase

EC=1.8.4.8
Alternative name(s):
3'-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAPS sulfotransferase
PAdoPS reductase
Gene names
Name:cysH
Ordered Locus Names:b2762, JW2732
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length244 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Reduction of activated sulfate into sulfite. HAMAP-Rule MF_00063

Catalytic activity

Adenosine 3',5'-bisphosphate + sulfite + thioredoxin disulfide = 3'-phosphoadenylyl sulfate + thioredoxin. HAMAP-Rule MF_00063

Pathway

Sulfur metabolism; hydrogen sulfide biosynthesis; sulfite from sulfate: step 3/3. HAMAP-Rule MF_00063

Subunit structure

Homodimer.

Subcellular location

Cytoplasm HAMAP-Rule MF_00063.

Sequence similarities

Belongs to the PAPS reductase family. CysH subfamily.

Binary interactions

With

Entry

#Exp.

IntAct

Notes

groLP0A6F51EBI-1114555,EBI-543750

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.5
Chain2 – 244243Phosphoadenosine phosphosulfate reductase HAMAP-Rule MF_00063
PRO_0000100630

Experimental info

Mutagenesis2091Y → F: Reduction in Vmax.
Mutagenesis2391C → S: 5-fold reduction in Vmax.
Sequence conflict271E → Q in AAA23652. Ref.2
Sequence conflict2261A → S in AAA23652. Ref.2

Secondary structure

........................................... 244
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P17854 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 7EC494ED2437E469

FASTA24427,976
        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 

« Hide

References

« Hide 'large scale' references
[1]"Characterisation of the gene cysH and of its product phospho-adenylylsulphate reductase from Escherichia coli."
Krone F.A., Westphal G., Schwenn J.D.
Mol. Gen. Genet. 225:314-319(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: K12.
[2]"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."
Ostrowski J., Wu J.-Y., Rueger D.C., Miller B.E., Siegel L.M., Kredich N.M.
J. Biol. Chem. 264:15726-15737(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: B.
[3]"The complete genome sequence of Escherichia coli K-12."
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.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[4]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"PAPS-reductase of Escherichia coli. Correlating the N-terminal amino acid sequence with the DNA of gene cys H."
Krone F.A., Westphal G., Meyer H.E., Schwenn J.D.
FEBS Lett. 260:6-9(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-18.
[6]"Reaction mechanism of thioredoxin: 3'-phospho-adenylylsulfate reductase investigated by site-directed mutagenesis."
Berendt U., Haverkamp T., Prior A., Schwenn J.D.
Eur. J. Biochem. 233:347-356(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION, MUTAGENESIS.
[7]"Crystal structure of phosphoadenylyl sulphate (PAPS) reductase: a new family of adenine nucleotide alpha hydrolases."
Savage H., Montoya G., Svensson C., Schwenn J.D., Sinning I.
Structure 5:895-906(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y07525 Genomic DNA. Translation: CAA68817.1.
M23008 Genomic DNA. Translation: AAA23652.1.
U29579 Genomic DNA. Translation: AAA69272.1.
U00096 Genomic DNA. Translation: AAC75804.1.
AP009048 Genomic DNA. Translation: BAE76839.1.
PIRRDECPA. S14221.
RefSeqNP_417242.1. NC_000913.3.
YP_490971.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1SURX-ray2.00A2-216[»]
2O8VX-ray3.00A1-244[»]
ProteinModelPortalP17854.
SMRP17854. Positions 2-244.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActP17854. 4 interactions.
STRING511145.b2762.

Proteomic databases

PaxDbP17854.
PRIDEP17854.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC75804; AAC75804; b2762.
BAE76839; BAE76839; BAE76839.
GeneID12932457.
947230.
KEGGecj:Y75_p2700.
eco:b2762.
PATRIC32120936. VBIEscCol129921_2860.

Organism-specific databases

EchoBASEEB0186.
EcoGeneEG10189. cysH.

Phylogenomic databases

eggNOGCOG0175.
HOGENOMHOG000249396.
KOK00390.
OMAPRNKLLD.
OrthoDBEOG6V1M7D.
PhylomeDBP17854.
ProtClustDBPRK02090.

Enzyme and pathway databases

BioCycEcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.
UniPathwayUPA00140; UER00206.

Gene expression databases

GenevestigatorP17854.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_00063. CysH.
InterProIPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01507. PAPS_reduct. 1 hit.
[Graphical view]
TIGRFAMsTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP17854.
PROP17854.

Entry information

Entry nameCYSH_ECOLI
AccessionPrimary (citable) accession number: P17854
Secondary accession number(s): Q2MA67
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 129 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene