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Protein

Aldehyde reductase YahK

Gene

yahK

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -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)DescriptionActionsGraphical viewLength
    Metal bindingi40Zinc 1; catalytic1
    Metal bindingi62Zinc 1; catalytic1
    Metal bindingi93Zinc 21
    Metal bindingi96Zinc 21
    Metal bindingi99Zinc 21
    Metal bindingi107Zinc 21
    Metal bindingi158Zinc 1; catalytic1

    GO - Molecular functioni

    • alcohol dehydrogenase (NADP+) activity Source: EcoCyc
    • zinc ion binding Source: InterPro

    Keywordsi

    Molecular functionOxidoreductase
    LigandMetal-binding, NADP, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:G6190-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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi
    • UP000000318 Componenti: Chromosome
    • UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG13595 yahK

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001608881 – 349Aldehyde reductase YahKAdd BLAST349

    Proteomic databases

    EPDiP75691
    PaxDbiP75691
    PRIDEiP75691

    2D gel databases

    SWISS-2DPAGEiP75691

    Interactioni

    Protein-protein interaction databases

    BioGridi4259802, 7 interactors
    DIPiDIP-11263N
    IntActiP75691, 10 interactors
    STRINGi316407.85674468

    Structurei

    Secondary structure

    1349
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi4 – 10Combined sources7
    Beta strandi16 – 19Combined sources4
    Beta strandi29 – 38Combined sources10
    Helixi41 – 48Combined sources8
    Beta strandi56 – 58Combined sources3
    Beta strandi64 – 71Combined sources8
    Beta strandi83 – 86Combined sources4
    Beta strandi88 – 91Combined sources4
    Beta strandi94 – 96Combined sources3
    Helixi97 – 100Combined sources4
    Helixi104 – 106Combined sources3
    Turni113 – 115Combined sources3
    Beta strandi128 – 136Combined sources9
    Helixi137 – 139Combined sources3
    Helixi147 – 149Combined sources3
    Helixi150 – 153Combined sources4
    Helixi154 – 157Combined sources4
    Helixi159 – 169Combined sources11
    Beta strandi177 – 181Combined sources5
    Helixi185 – 196Combined sources12
    Beta strandi200 – 207Combined sources8
    Helixi208 – 210Combined sources3
    Helixi211 – 217Combined sources7
    Beta strandi220 – 224Combined sources5
    Helixi228 – 232Combined sources5
    Turni233 – 236Combined sources4
    Beta strandi238 – 243Combined sources6
    Helixi251 – 255Combined sources5
    Beta strandi258 – 266Combined sources9
    Helixi279 – 283Combined sources5
    Turni284 – 286Combined sources3
    Beta strandi288 – 291Combined sources4
    Helixi297 – 310Combined sources14
    Beta strandi316 – 319Combined sources4
    Helixi321 – 323Combined sources3
    Helixi324 – 332Combined sources9
    Beta strandi336 – 343Combined sources8
    Helixi344 – 347Combined sources4

    3D structure databases

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

    Miscellaneous databases

    EvolutionaryTraceiP75691

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiENOG4105DQ4 Bacteria
    COG1064 LUCA
    HOGENOMiHOG000294667
    InParanoidiP75691
    KOiK13979
    OMAiYRFSIDM
    PhylomeDBiP75691

    Family and domain databases

    InterProiView protein in InterPro
    IPR013149 ADH_C
    IPR013154 ADH_N
    IPR002328 ADH_Zn_CS
    IPR029752 D-isomer_DH_CS1
    IPR011032 GroES-like_sf
    IPR036291 NAD(P)-bd_dom_sf
    IPR020843 PKS_ER
    PfamiView protein in Pfam
    PF08240 ADH_N, 1 hit
    PF00107 ADH_zinc_N, 1 hit
    SMARTiView protein in SMART
    SM00829 PKS_ER, 1 hit
    SUPFAMiSSF50129 SSF50129, 1 hit
    SSF51735 SSF51735, 1 hit
    PROSITEiView protein in PROSITE
    PS00059 ADH_ZINC, 1 hit

    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)DescriptionActionsGraphical viewLength
    Sequence conflicti116S → L in AAB18051 (Ref. 1) Curated1
    Sequence conflicti145H → Y in AAB18051 (Ref. 1) Curated1

    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
    PATRICifig|1411691.4.peg.1952

    Similar proteinsi

    Entry informationi

    Entry nameiYAHK_ECOLI
    AccessioniPrimary (citable) accession number: P75691
    Secondary accession number(s): P71306, Q2MC98
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: March 28, 2018
    This is version 146 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome
    UniProt is an ELIXIR core data resource
    Main funding by: National Institutes of Health