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P17854

- CYSH_ECOLI

UniProt

P17854 - CYSH_ECOLI

Protein

Phosphoadenosine phosphosulfate reductase

Gene

cysH

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    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

    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-SubCell

    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.
    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

    MSKLDLNALN ELPKVDRILA LAETNAELEK LDAEGRVAWA LDNLPGEYVL    50
    SSSFGIQAAV SLHLVNQIRP DIPVILTDTG YLFPETYRFI DELTDKLKLN 100
    LKVYRATESA AWQEARYGKL WEQGVEGIEK YNDINKVEPM NRALKELNAQ 150
    TWFAGLRREQ SGSRANLPVL AIQRGVFKVL PIIDWDNRTI YQYLQKHGLK 200
    YHPLWDEGYL SVGDTHTTRK WEPGMAEEET RFFGLKRECG LHEG 244
    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.
    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

    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 1, 2014
    This is version 131 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