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Protein

Aldehyde reductase Ahr

Gene

ahr

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 including aliphatic fatty aldehydes (C4-C16), into their corresponding alcohols. Has a strong preference for NADPH over NADH as the electron donor. Cannot use glyceraldehyde or a ketone as substrate. Is a relevant source of NADPH-dependent aldehyde reductase activity in E.coli. The in vivo functions of Ahr has yet to be determined.3 Publications

Catalytic activityi

An alcohol + NADP+ = an aldehyde + NADPH.2 Publications

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit.1 Publication

Kineticsi

kcat is 333 sec(-1) for acetaldehyde reduction. kcat is 207 sec(-1) for propionaldehyde reduction. kcat is 464 sec(-1) for butyraldehyde reduction. kcat is 51 sec(-1) for isobutyraldehyde reduction. kcat is 78 sec(-1) for crotonaldehyde reduction. kcat is 312 sec(-1) for glutaraldehyde reduction. kcat is 2.6 sec(-1) for 5-hydroxyvalerate reduction. kcat is 419 sec(-1) for hexanaldehyde reduction. kcat is 313 sec(-1) for benzaldehyde reduction. kcat is 224 sec(-1) for furfural reduction. kcat is 13.8 sec(-1) for butanol oxidation. kcat is 12.9 sec(-1) for 1,4-butanediol oxidation.

  1. KM=73.4 mM for acetaldehyde1 Publication
  2. KM=19.6 mM for propionaldehyde1 Publication
  3. KM=2.1 mM for butyraldehyde1 Publication
  4. KM=193.7 mM for isobutyraldehyde1 Publication
  5. KM=2.4 mM for crotonaldehyde1 Publication
  6. KM=5.8 mM for glutaraldehyde1 Publication
  7. KM=59.7 mM for 5-hydroxyvalerate1 Publication
  8. KM=0.34 mM for hexanaldehyde1 Publication
  9. KM=0.24 mM for benzaldehyde1 Publication
  10. KM=0.22 mM for furfural1 Publication
  11. KM=3.5 mM for butanol1 Publication
  12. KM=24.1 mM for 1,4-butanediol1 Publication
  13. KM=0.06 mM for NADPH1 Publication
  14. KM=0.076 mM for NADP+1 Publication

    Temperature dependencei

    Optimum temperature is 37-50 degrees Celsius using butyraldehyde as substrate.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi38 – 381Zinc 1; catalyticBy similarity
    Metal bindingi63 – 631Zinc 1; catalyticBy similarity
    Metal bindingi96 – 961Zinc 2By similarity
    Metal bindingi99 – 991Zinc 2By similarity
    Metal bindingi102 – 1021Zinc 2By similarity
    Metal bindingi110 – 1101Zinc 2By similarity
    Metal bindingi152 – 1521Zinc 1; catalyticBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Fatty acid metabolism, Lipid metabolism

    Keywords - Ligandi

    Metal-binding, NADP, Zinc

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11436-MONOMER.
    ECOL316407:JW5761-MONOMER.
    MetaCyc:EG11436-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Aldehyde reductase Ahr (EC:1.1.1.2)
    Alternative name(s):
    Zinc-dependent alcohol dehydrogenase Ahr
    Gene namesi
    Name:ahr
    Synonyms:yjgB
    Ordered Locus Names:b4269, JW5761
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318 Componenti: Chromosome UP000000625 Componenti: Chromosome

    Organism-specific databases

    EcoGeneiEG11436. ahr.

    Pathology & Biotechi

    Biotechnological usei

    This enzyme can be applied to the microbial production of fatty alcohols that have numerous applications as fuels, fragrances, emollients, food additives, and detergents. Thus, together with complementing enzymes, the broad substrate specificity of Ahr opens the road for direct and tailored enzyme-catalyzed conversion of lipids into user-ready chemical commodities.1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 339339Aldehyde reductase AhrPRO_0000160894Add
    BLAST

    Proteomic databases

    PaxDbiP27250.
    PRIDEiP27250.

    Expressioni

    Gene expression databases

    GenevestigatoriP27250.

    Interactioni

    Protein-protein interaction databases

    STRINGi511145.b4269.

    Structurei

    3D structure databases

    ProteinModelPortaliP27250.
    SMRiP27250. Positions 7-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiCOG1064.
    HOGENOMiHOG000294667.
    InParanoidiP27250.
    KOiK12957.
    OMAiDKIRANW.
    OrthoDBiEOG66XBFN.
    PhylomeDBiP27250.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    P27250-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MSMIKSYAAK EAGGELEVYE YDPGELRPQD VEVQVDYCGI CHSDLSMIDN
    60 70 80 90 100
    EWGFSQYPLV AGHEVIGRVV ALGSAAQDKG LQVGQRVGIG WTARSCGHCD
    110 120 130 140 150
    ACISGNQINC EQGAVPTIMN RGGFAEKLRA DWQWVIPLPE NIDIESAGPL
    160 170 180 190 200
    LCGGITVFKP LLMHHITATS RVGVIGIGGL GHIAIKLLHA MGCEVTAFSS
    210 220 230 240 250
    NPAKEQEVLA MGADKVVNSR DPQALKALAG QFDLIINTVN VSLDWQPYFE
    260 270 280 290 300
    ALTYGGNFHT VGAVLTPLSV PAFTLIAGDR SVSGSATGTP YELRKLMRFA
    310 320 330
    ARSKVAPTTE LFPMSKINDA IQHVRDGKAR YRVVLKADF
    Length:339
    Mass (Da):36,502
    Last modified:February 1, 1995 - v2
    Checksum:i0854DDEFA16B9EEE
    GO

    Sequence cautioni

    The sequence AAA97166.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.Curated

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti331 – 3399YRVVLKADF → TAWC in AAA72122 (Ref. 1) Curated

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M96355 Genomic DNA. Translation: AAA72122.1.
    U14003 Genomic DNA. Translation: AAA97166.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77226.2.
    AP009048 Genomic DNA. Translation: BAE78266.1.
    PIRiS56495.
    RefSeqiNP_418690.4. NC_000913.3.

    Genome annotation databases

    EnsemblBacteriaiAAC77226; AAC77226; b4269.
    BAE78266; BAE78266; BAE78266.
    GeneIDi948802.
    KEGGiecj:Y75_p4152.
    eco:b4269.
    PATRICi32124111. VBIEscCol129921_4400.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    M96355 Genomic DNA. Translation: AAA72122.1.
    U14003 Genomic DNA. Translation: AAA97166.1. Different initiation.
    U00096 Genomic DNA. Translation: AAC77226.2.
    AP009048 Genomic DNA. Translation: BAE78266.1.
    PIRiS56495.
    RefSeqiNP_418690.4. NC_000913.3.

    3D structure databases

    ProteinModelPortaliP27250.
    SMRiP27250. Positions 7-335.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi511145.b4269.

    Proteomic databases

    PaxDbiP27250.
    PRIDEiP27250.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC77226; AAC77226; b4269.
    BAE78266; BAE78266; BAE78266.
    GeneIDi948802.
    KEGGiecj:Y75_p4152.
    eco:b4269.
    PATRICi32124111. VBIEscCol129921_4400.

    Organism-specific databases

    EchoBASEiEB1406.
    EcoGeneiEG11436. ahr.

    Phylogenomic databases

    eggNOGiCOG1064.
    HOGENOMiHOG000294667.
    InParanoidiP27250.
    KOiK12957.
    OMAiDKIRANW.
    OrthoDBiEOG66XBFN.
    PhylomeDBiP27250.

    Enzyme and pathway databases

    BioCyciEcoCyc:EG11436-MONOMER.
    ECOL316407:JW5761-MONOMER.
    MetaCyc:EG11436-MONOMER.

    Miscellaneous databases

    PROiP27250.

    Gene expression databases

    GenevestigatoriP27250.

    Family and domain databases

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

    Publicationsi

    « Hide 'large scale' publications
    1. Pucci M.J., Discotto L.F., Dougherty T.J.
      Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: B.
    2. "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes."
      Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.
      Nucleic Acids Res. 23:2105-2119(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, ZINC-BINDING, COFACTOR.
    6. "Isobutyraldehyde production from Escherichia coli by removing aldehyde reductase activity."
      Rodriguez G.M., Atsumi S.
      Microb. Cell Fact. 11:90-90(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    7. "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 BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, 3D-STRUCTURE MODELING.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
    8. "Carboxylic acid reductase is a versatile enzyme for the conversion of fatty acids into fuels and chemical commodities."
      Akhtar M.K., Turner N.J., Jones P.R.
      Proc. Natl. Acad. Sci. U.S.A. 110:87-92(2013) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, GENE NAME, BIOTECHNOLOGY.
      Strain: B / BL21-DE3.

    Entry informationi

    Entry nameiAHR_ECOLI
    AccessioniPrimary (citable) accession number: P27250
    Secondary accession number(s): P76812, Q2M640
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1992
    Last sequence update: February 1, 1995
    Last modified: May 27, 2015
    This is version 118 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. 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.