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Protein

Phosphoadenosine phosphosulfate reductase

Gene

cysH

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: 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.
BRENDAi1.8.4.8. 2026.
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 Componenti: Chromosome UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10189. cysH.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
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 – 105Combined sources
Helixi14 – 2815Combined sources
Helixi33 – 4311Combined sources
Beta strandi46 – 516Combined sources
Turni56 – 583Combined sources
Helixi59 – 6810Combined sources
Beta strandi73 – 786Combined sources
Helixi84 – 9613Combined sources
Beta strandi100 – 1056Combined sources
Helixi110 – 1178Combined sources
Helixi120 – 1223Combined sources
Helixi124 – 13512Combined sources
Helixi137 – 14610Combined sources
Beta strandi149 – 1535Combined sources
Beta strandi160 – 1623Combined sources
Turni163 – 1664Combined sources
Beta strandi169 – 1735Combined sources
Beta strandi176 – 1794Combined sources
Turni181 – 1844Combined sources
Helixi187 – 19711Combined sources
Helixi203 – 2075Combined sources
Turni216 – 2183Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
OMAiPRNKLLD.
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]
PIRSFiPIRSF000857. PAPS_reductase. 1 hit.
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 22, 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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

IntActiP17854. 4 interactions.
STRINGi511145.b2762.

Proteomic databases

PaxDbiP17854.
PRIDEiP17854.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

EchoBASEiEB0186.
EcoGeneiEG10189. cysH.

Phylogenomic databases

eggNOGiCOG0175.
HOGENOMiHOG000249396.
InParanoidiP17854.
KOiK00390.
OMAiPRNKLLD.
OrthoDBiEOG6V1M7D.
PhylomeDBiP17854.

Enzyme and pathway databases

UniPathwayiUPA00140; UER00206.
BioCyciEcoCyc:PAPSSULFOTRANS-MONOMER.
ECOL316407:JW2732-MONOMER.
MetaCyc:PAPSSULFOTRANS-MONOMER.
BRENDAi1.8.4.8. 2026.

Miscellaneous databases

EvolutionaryTraceiP17854.
PROiP17854.

Gene expression databases

GenevestigatoriP17854.

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]
PIRSFiPIRSF000857. PAPS_reductase. 1 hit.
TIGRFAMsiTIGR00434. cysH. 1 hit.
TIGR02057. PAPS_reductase. 1 hit.
ProtoNetiSearch...

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(1990) [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(1988) [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(2005) [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(1989) [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(1994) [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(1996) [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: October 31, 1990
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 135 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.