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Protein

Aldehyde reductase YahK

Gene

yahK

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

Functioni

Catalyzes the reduction of a wide range of aldehydes into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use a ketone as substrate. Is a major source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of YahK has yet to be determined.1 Publication

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.1 Publication

Cofactori

Zn2+2 PublicationsNote: Binds 2 Zn2+ ions per subunit.2 Publications

Kineticsi

kcat is 11.2 sec(-1) for acetaldehyde reduction. kcat is 11.6 sec(-1) for propionaldehyde reduction. kcat is 12.3 sec(-1) for glyceraldehyde reduction. kcat is 41.6 sec(-1) for butyraldehyde reduction. kcat is 32.1 sec(-1) for isobutyraldehyde reduction. kcat is 32.6 sec(-1) for crotonaldehyde reduction. kcat is 13.4 sec(-1) for glutaraldehyde reduction. kcat is 0.18 sec(-1) for 5-hydroxyvalerate reduction. kcat is 18.3 sec(-1) for hexanaldehyde reduction. kcat is 7.75 sec(-1) for benzaldehyde reduction. kcat is 12.5 sec(-1) for furfural reduction. kcat is 4.7 sec(-1) for butanol oxidation. kcat is 6.7 sec(-1) for 1,4-butanediol oxidation.

  1. KM=13.3 mM for acetaldehyde1 Publication
  2. KM=10.9 mM for propionaldehyde1 Publication
  3. KM=4.4 mM for glyceraldehyde1 Publication
  4. KM=2.1 mM for butyraldehyde1 Publication
  5. KM=2.2 mM for isobutyraldehyde1 Publication
  6. KM=3.6 mM for crotonaldehyde1 Publication
  7. KM=4.1 mM for glutaraldehyde1 Publication
  8. KM=52.6 mM for 5-hydroxyvalerate1 Publication
  9. KM=0.37 mM for hexanaldehyde1 Publication
  10. KM=0.29 mM for benzaldehyde1 Publication
  11. KM=0.135 mM for furfural1 Publication
  12. KM=6.6 mM for butanol1 Publication
  13. KM=38.5 mM for 1,4-butanediol1 Publication
  14. KM=0.011 mM for NADPH1 Publication
  15. KM=0.012 mM for NADP+1 Publication

    Temperature dependencei

    Shows a constant increase in activity until 60 degrees Celsius using butyraldehyde as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi40 – 401Zinc 1; catalytic
    Metal bindingi62 – 621Zinc 1; catalytic
    Metal bindingi93 – 931Zinc 2
    Metal bindingi96 – 961Zinc 2
    Metal bindingi99 – 991Zinc 2
    Metal bindingi107 – 1071Zinc 2
    Metal bindingi158 – 1581Zinc 1; catalytic

    GO - Molecular functioni

    • alcohol dehydrogenase (NADP+) activity Source: EcoCyc
    • zinc ion binding Source: InterPro
    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    Metal-binding, NADP, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:G6190-MONOMER.
    ECOL316407:JW0317-MONOMER.
    MetaCyc:G6190-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde reductase YahK (EC:1.1.1.2)
    Alternative name(s):
    Zinc-dependent alcohol dehydrogenase YahK
    Gene namesi
    Name:yahK
    Ordered Locus Names:b0325, JW0317
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13595. yahK.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 349349Aldehyde reductase YahKPRO_0000160888Add
    BLAST

    Proteomic databases

    EPDiP75691.
    PaxDbiP75691.
    PRIDEiP75691.

    2D gel databases

    SWISS-2DPAGEP75691.

    Interactioni

    Protein-protein interaction databases

    BioGridi4259802. 7 interactions.
    DIPiDIP-11263N.
    IntActiP75691. 9 interactions.
    STRINGi511145.b0325.

    Structurei

    Secondary structure

    1
    349
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi4 – 107Combined sources
    Beta strandi16 – 194Combined sources
    Beta strandi29 – 3810Combined sources
    Helixi41 – 488Combined sources
    Beta strandi56 – 583Combined sources
    Beta strandi64 – 718Combined sources
    Beta strandi83 – 864Combined sources
    Beta strandi88 – 914Combined sources
    Beta strandi94 – 963Combined sources
    Helixi97 – 1004Combined sources
    Helixi104 – 1063Combined sources
    Turni113 – 1153Combined sources
    Beta strandi128 – 1369Combined sources
    Helixi137 – 1393Combined sources
    Helixi147 – 1493Combined sources
    Helixi150 – 1534Combined sources
    Helixi154 – 1574Combined sources
    Helixi159 – 16911Combined sources
    Beta strandi177 – 1815Combined sources
    Helixi185 – 19612Combined sources
    Beta strandi200 – 2078Combined sources
    Helixi208 – 2103Combined sources
    Helixi211 – 2177Combined sources
    Beta strandi220 – 2245Combined sources
    Helixi228 – 2325Combined sources
    Turni233 – 2364Combined sources
    Beta strandi238 – 2436Combined sources
    Helixi251 – 2555Combined sources
    Beta strandi258 – 2669Combined sources
    Helixi279 – 2835Combined sources
    Turni284 – 2863Combined sources
    Beta strandi288 – 2914Combined sources
    Helixi297 – 31014Combined sources
    Beta strandi316 – 3194Combined sources
    Helixi321 – 3233Combined sources
    Helixi324 – 3329Combined sources
    Beta strandi336 – 3438Combined sources
    Helixi344 – 3474Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UUFX-ray1.76A2-349[»]
    ProteinModelPortaliP75691.
    SMRiP75691. Positions 3-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP75691.

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DQ4. Bacteria.
    COG1064. LUCA.
    HOGENOMiHOG000294667.
    InParanoidiP75691.
    KOiK13979.
    OMAiYCTGGGM.
    OrthoDBiEOG66XBFN.
    PhylomeDBiP75691.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR029752. D-isomer_DH_CS1.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    P75691-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKIKAVGAYS AKQPLEPMDI TRREPGPNDV KIEIAYCGVC HSDLHQVRSE
    60 70 80 90 100
    WAGTVYPCVP GHEIVGRVVA VGDQVEKYAP GDLVGVGCIV DSCKHCEECE
    110 120 130 140 150
    DGLENYCDHM TGTYNSPTPD EPGHTLGGYS QQIVVHERYV LRIRHPQEQL
    160 170 180 190 200
    AAVAPLLCAG ITTYSPLRHW QAGPGKKVGV VGIGGLGHMG IKLAHAMGAH
    210 220 230 240 250
    VVAFTTSEAK REAAKALGAD EVVNSRNADE MAAHLKSFDF ILNTVAAPHN
    260 270 280 290 300
    LDDFTTLLKR DGTMTLVGAP ATPHKSPEVF NLIMKRRAIA GSMIGGIPET
    310 320 330 340
    QEMLDFCAEH GIVADIEMIR ADQINEAYER MLRGDVKYRF VIDNRTLTD
    Length:349
    Mass (Da):37,978
    Last modified:February 1, 1997 - v1
    Checksum:iAD0E2DF4D43C9B09
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti116 – 1161S → L in AAB18051 (Ref. 1) Curated
    Sequence conflicti145 – 1451H → Y in AAB18051 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U73857 Genomic DNA. Translation: AAB18051.1.
    U00096 Genomic DNA. Translation: AAC73428.1.
    AP009048 Genomic DNA. Translation: BAE76108.1.
    PIRiE64759.
    RefSeqiNP_414859.1. NC_000913.3.
    WP_000692754.1. NZ_LN832404.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73428; AAC73428; b0325.
    BAE76108; BAE76108; BAE76108.
    GeneIDi944975.
    KEGGiecj:JW0317.
    eco:b0325.
    PATRICi32115779. VBIEscCol129921_0332.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U73857 Genomic DNA. Translation: AAB18051.1.
    U00096 Genomic DNA. Translation: AAC73428.1.
    AP009048 Genomic DNA. Translation: BAE76108.1.
    PIRiE64759.
    RefSeqiNP_414859.1. NC_000913.3.
    WP_000692754.1. NZ_LN832404.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UUFX-ray1.76A2-349[»]
    ProteinModelPortaliP75691.
    SMRiP75691. Positions 3-348.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    BioGridi4259802. 7 interactions.
    DIPiDIP-11263N.
    IntActiP75691. 9 interactions.
    STRINGi511145.b0325.

    2D gel databases

    SWISS-2DPAGEP75691.

    Proteomic databases

    EPDiP75691.
    PaxDbiP75691.
    PRIDEiP75691.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC73428; AAC73428; b0325.
    BAE76108; BAE76108; BAE76108.
    GeneIDi944975.
    KEGGiecj:JW0317.
    eco:b0325.
    PATRICi32115779. VBIEscCol129921_0332.

    Organism-specific databases

    EchoBASEiEB3364.
    EcoGeneiEG13595. yahK.

    Phylogenomic databases

    eggNOGiENOG4105DQ4. Bacteria.
    COG1064. LUCA.
    HOGENOMiHOG000294667.
    InParanoidiP75691.
    KOiK13979.
    OMAiYCTGGGM.
    OrthoDBiEOG66XBFN.
    PhylomeDBiP75691.

    Enzyme and pathway databases

    BioCyciEcoCyc:G6190-MONOMER.
    ECOL316407:JW0317-MONOMER.
    MetaCyc:G6190-MONOMER.

    Miscellaneous databases

    EvolutionaryTraceiP75691.
    PROiP75691.

    Family and domain databases

    Gene3Di3.40.50.720. 1 hit.
    3.90.180.10. 1 hit.
    InterProiIPR013149. ADH_C.
    IPR013154. ADH_N.
    IPR002085. ADH_SF_Zn-type.
    IPR002328. ADH_Zn_CS.
    IPR029752. D-isomer_DH_CS1.
    IPR011032. GroES-like.
    IPR016040. NAD(P)-bd_dom.
    IPR020843. PKS_ER.
    [Graphical view]
    PANTHERiPTHR11695. PTHR11695. 1 hit.
    PfamiPF08240. ADH_N. 1 hit.
    PF00107. ADH_zinc_N. 1 hit.
    [Graphical view]
    SMARTiSM00829. PKS_ER. 1 hit.
    [Graphical view]
    SUPFAMiSSF50129. SSF50129. 1 hit.
    SSF51735. SSF51735. 1 hit.
    PROSITEiPS00059. ADH_ZINC. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Sequence of minutes 4-25 of Escherichia coli."
      Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
      Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    3. "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.
    4. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ZINC-BINDING, COFACTOR.
    5. "Novel CAD-like enzymes from Escherichia coli K-12 as additional tools in chemical production."
      Pick A., Ruhmann B., Schmid J., Sieber V.
      Appl. Microbiol. Biotechnol. 97:5815-5824(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    6. "Crystal structure of yahK, a zinc-type alcohol dehydrogenase-like protein."
      Jeudy S., Claverie J.-M., Abergel C.
      Submitted (DEC-2003) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ZINC IONS, COFACTOR.

    Entry informationi

    Entry nameiYAHK_ECOLI
    AccessioniPrimary (citable) accession number: P75691
    Secondary accession number(s): P71306, Q2MC98
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: May 11, 2016
    This is version 135 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

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

    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 one 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.