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P17854

- CYSH_ECOLI

UniProt

P17854 - CYSH_ECOLI

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Protein

Phosphoadenosine phosphosulfate reductase

Gene

cysH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Reduction of activated sulfate into sulfite.

Catalytic activityi

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

Pathwayi

GO - Molecular functioni

  1. phosphoadenylyl-sulfate reductase (thioredoxin) activity Source: EcoCyc

GO - Biological processi

  1. cysteine biosynthetic process Source: InterPro
  2. hydrogen sulfide biosynthetic process Source: UniProtKB-UniPathway
  3. methionine biosynthetic process Source: InterPro
  4. sulfate assimilation, phosphoadenylyl sulfate reduction by phosphoadenylyl-sulfate reductase (thioredoxin) Source: EcoCyc
  5. sulfur compound metabolic process Source: EcoCyc
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Enzyme and pathway databases

BioCyciEcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.
UniPathwayiUPA00140; UER00206.

Names & Taxonomyi

Protein namesi
Recommended name:
Phosphoadenosine phosphosulfate reductase (EC:1.8.4.8)
Alternative name(s):
3'-phosphoadenylylsulfate reductase
PAPS reductase, thioredoxin dependent
PAPS sulfotransferase
PAdoPS reductase
Gene namesi
Name:cysH
Ordered Locus Names:b2762, JW2732
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

Organism-specific databases

EcoGeneiEG10189. cysH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091Y → F: Reduction in Vmax. 1 Publication
Mutagenesisi239 – 2391C → S: 5-fold reduction in Vmax. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 244243Phosphoadenosine phosphosulfate reductasePRO_0000100630Add
BLAST

Proteomic databases

PaxDbiP17854.
PRIDEiP17854.

Expressioni

Gene expression databases

GenevestigatoriP17854.

Interactioni

Subunit structurei

Homodimer.

Binary interactionsi

WithEntry#Exp.IntActNotes
groLP0A6F51EBI-1114555,EBI-543750

Protein-protein interaction databases

IntActiP17854. 4 interactions.
STRINGi511145.b2762.

Structurei

Secondary structure

1
244
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi6 – 105
Helixi14 – 2815
Helixi33 – 4311
Beta strandi46 – 516
Turni56 – 583
Helixi59 – 6810
Beta strandi73 – 786
Helixi84 – 9613
Beta strandi100 – 1056
Helixi110 – 1178
Helixi120 – 1223
Helixi124 – 13512
Helixi137 – 14610
Beta strandi149 – 1535
Beta strandi160 – 1623
Turni163 – 1664
Beta strandi169 – 1735
Beta strandi176 – 1794
Turni181 – 1844
Helixi187 – 19711
Helixi203 – 2075
Turni216 – 2183

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1SURX-ray2.00A2-216[»]
2O8VX-ray3.00A1-244[»]
ProteinModelPortaliP17854.
SMRiP17854. Positions 2-244.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP17854.

Family & Domainsi

Sequence similaritiesi

Belongs to the PAPS reductase family. CysH subfamily.Curated

Phylogenomic databases

eggNOGiCOG0175.
HOGENOMiHOG000249396.
InParanoidiP17854.
KOiK00390.
OMAiQSPAWQE.
OrthoDBiEOG6V1M7D.
PhylomeDBiP17854.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_00063. CysH.
InterProiIPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01507. PAPS_reduct. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P17854-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL
60 70 80 90 100
SSSFGIQAAV SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN
110 120 130 140 150
LKVYRATESA AWQEARYGKL WEQGVEGIEK YNDINKVEPM NRALKELNAQ
160 170 180 190 200
TWFAGLRREQ SGSRANLPVL AIQRGVFKVL PIIDWDNRTI YQYLQKHGLK
210 220 230 240
YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG
Length:244
Mass (Da):27,976
Last modified:January 23, 2007 - v3
Checksum:i7EC494ED2437E469
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti27 – 271E → Q in AAA23652. (PubMed:2670946)Curated
Sequence conflicti226 – 2261A → S in AAA23652. (PubMed:2670946)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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.
PIRiS14221. RDECPA.
RefSeqiNP_417242.1. NC_000913.3.
YP_490971.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC75804; AAC75804; b2762.
BAE76839; BAE76839; BAE76839.
GeneIDi12932457.
947230.
KEGGiecj:Y75_p2700.
eco:b2762.
PATRICi32120936. VBIEscCol129921_2860.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
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 .
PIRi S14221. RDECPA.
RefSeqi NP_417242.1. NC_000913.3.
YP_490971.1. NC_007779.1.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1SUR X-ray 2.00 A 2-216 [» ]
2O8V X-ray 3.00 A 1-244 [» ]
ProteinModelPortali P17854.
SMRi P17854. Positions 2-244.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

IntActi P17854. 4 interactions.
STRINGi 511145.b2762.

Proteomic databases

PaxDbi P17854.
PRIDEi P17854.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC75804 ; AAC75804 ; b2762 .
BAE76839 ; BAE76839 ; BAE76839 .
GeneIDi 12932457.
947230.
KEGGi ecj:Y75_p2700.
eco:b2762.
PATRICi 32120936. VBIEscCol129921_2860.

Organism-specific databases

EchoBASEi EB0186.
EcoGenei EG10189. cysH.

Phylogenomic databases

eggNOGi COG0175.
HOGENOMi HOG000249396.
InParanoidi P17854.
KOi K00390.
OMAi QSPAWQE.
OrthoDBi EOG6V1M7D.
PhylomeDBi P17854.

Enzyme and pathway databases

UniPathwayi UPA00140 ; UER00206 .
BioCyci EcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.

Miscellaneous databases

EvolutionaryTracei P17854.
PROi P17854.

Gene expression databases

Genevestigatori P17854.

Family and domain databases

Gene3Di 3.40.50.620. 1 hit.
HAMAPi MF_00063. CysH.
InterProi IPR004511. PAPS/APS_Rdtase.
IPR002500. PAPS_reduct.
IPR011800. PAPS_reductase_CysH.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view ]
Pfami PF01507. PAPS_reduct. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. 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).

Entry informationi

Entry nameiCYSH_ECOLI
AccessioniPrimary (citable) accession number: P17854
Secondary accession number(s): Q2MA67
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: October 29, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3