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Reviewed, UniProtKB/Swiss-Prot P17854 (CYSH_ECOLI)

Last modified June 16, 2009. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Phosphoadenosine phosphosulfate reductase
    EC=1.8.4.8
Alternative name(s):
    PAPS reductase, thioredoxin dependent
    PAdoPS reductase
    3'-phosphoadenylylsulfate reductase
    PAPS sulfotransferase
Gene names
Name: cysH
Ordered Locus Names: b2762, JW2732
OrganismEscherichia coli (strain K12) [Complete 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 MF_00063

Catalytic activity

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

Pathway

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

Subunit structure

Homodimer. HAMAP MF_00063

Subcellular location

Cytoplasm. HAMAP 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 MF_00063
PRO_0000100630

Experimental info

Mutagenesis2091Y → F: Reduction in Vmax. HAMAP MF_00063
Mutagenesis2391C → S: 5-fold reduction in Vmax. HAMAP MF_00063
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
P17854-1 [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: 2005873] [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: 2670946] [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 277:1453-1474(1997) [PubMed: 9278503] [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: 16738553] [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: 2404794] [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: 7588765] [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: 9261082] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
+Additional computationally mapped references.

Cross-references

Sequence databases

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.
RefSeqAP_003329.1.
NP_417242.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1SURX-ray2.00A2-216[»]
2O8VX-ray3.00A1-244[»]
ModBaseSearch...

Protein-protein interaction databases

IntActP17854. 4 interactions.

Genome annotation databases

GeneID947230.
GenomeReviewsGene locus JW2732 in contig AP009048_GR.
Gene locus b2762 in contig U00096_GR.
KEGGecj:JW2732.
eco:b2762.

Organism-specific databases

EchoBASEEB0186.
EcoGeneEG10189. cysH.
CMRSearch...

Phylogenomic databases

HOGENOMP17854.
OMAP17854. TRFNGLK.

Enzyme and pathway databases

BioCycEcoCyc:PAPSSULFOTRANS-MON.
MetaCyc:PAPSSULFOTRANS-MON.

Family and domain databases

HAMAPMF_00063.
[Tree]
InterProIPR004511. PAdo_PSO4_Rdtase_CysH.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
Gene3DG3DSA:3.40.50.620. Rossmann-like_a/b/a_fold. 1 hit.
PfamPF01507. PAPS_reduct. 1 hit.
[Graphical view]
TIGRFAMsTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNetSearch...

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: June 16, 2009
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Escherichia coli

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

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents