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P27250 (AHR_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde reductase Ahr

EC=1.1.1.2
Alternative name(s):
Zinc-dependent alcohol dehydrogenase Ahr
Gene names
Name:ahr
Synonyms:yjgB
Ordered Locus Names:b4269, JW5761
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.7 Ref.8

Catalytic activity

An alcohol + NADP+ = an aldehyde + NADPH. Ref.7 Ref.8

Cofactor

Binds 2 zinc ions per subunit Probable. Ref.5

Biotechnological use

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. Ref.8

Sequence similarities

Belongs to the zinc-containing alcohol dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

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.

KM=73.4 mM for acetaldehyde Ref.7

KM=19.6 mM for propionaldehyde

KM=2.1 mM for butyraldehyde

KM=193.7 mM for isobutyraldehyde

KM=2.4 mM for crotonaldehyde

KM=5.8 mM for glutaraldehyde

KM=59.7 mM for 5-hydroxyvalerate

KM=0.34 mM for hexanaldehyde

KM=0.24 mM for benzaldehyde

KM=0.22 mM for furfural

KM=3.5 mM for butanol

KM=24.1 mM for 1,4-butanediol

KM=0.06 mM for NADPH

KM=0.076 mM for NADP+

Temperature dependence:

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

Sequence caution

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 339339Aldehyde reductase Ahr
PRO_0000160894

Sites

Metal binding381Zinc 1; catalytic By similarity
Metal binding631Zinc 1; catalytic By similarity
Metal binding961Zinc 2 By similarity
Metal binding991Zinc 2 By similarity
Metal binding1021Zinc 2 By similarity
Metal binding1101Zinc 2 By similarity
Metal binding1521Zinc 1; catalytic By similarity

Experimental info

Sequence conflict331 – 3399YRVVLKADF → TAWC in AAA72122. Ref.1

Sequences

Sequence LengthMass (Da)Tools
P27250 [UniParc].

Last modified February 1, 1995. Version 2.
Checksum: 0854DDEFA16B9EEE

FASTA33936,502
        10         20         30         40         50         60 
MSMIKSYAAK EAGGELEVYE YDPGELRPQD VEVQVDYCGI CHSDLSMIDN EWGFSQYPLV 

        70         80         90        100        110        120 
AGHEVIGRVV ALGSAAQDKG LQVGQRVGIG WTARSCGHCD ACISGNQINC EQGAVPTIMN 

       130        140        150        160        170        180 
RGGFAEKLRA DWQWVIPLPE NIDIESAGPL LCGGITVFKP LLMHHITATS RVGVIGIGGL 

       190        200        210        220        230        240 
GHIAIKLLHA MGCEVTAFSS NPAKEQEVLA MGADKVVNSR DPQALKALAG QFDLIINTVN 

       250        260        270        280        290        300 
VSLDWQPYFE ALTYGGNFHT VGAVLTPLSV PAFTLIAGDR SVSGSATGTP YELRKLMRFA 

       310        320        330 
ARSKVAPTTE LFPMSKINDA IQHVRDGKAR YRVVLKADF 

« Hide

References

« Hide 'large scale' references
[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]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
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]"Exploring the microbial metalloproteome using MIRAGE."
Sevcenco A.M., Pinkse M.W., Wolterbeek H.T., Verhaert P.D., Hagen W.R., Hagedoorn P.L.
Metallomics 3:1324-1330(2011) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRS56495.
RefSeqNP_418690.4. NC_000913.3.
YP_492407.1. NC_007779.1.

3D structure databases

ProteinModelPortalP27250.
SMRP27250. Positions 7-335.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING511145.b4269.

Proteomic databases

PaxDbP27250.
PRIDEP27250.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC77226; AAC77226; b4269.
BAE78266; BAE78266; BAE78266.
GeneID12934055.
948802.
KEGGecj:Y75_p4152.
eco:b4269.
PATRIC32124111. VBIEscCol129921_4400.

Organism-specific databases

EchoBASEEB1406.
EcoGeneEG11436. ahr.

Phylogenomic databases

eggNOGCOG1064.
HOGENOMHOG000294667.
KOK12957.
OMAVESCGIC.
OrthoDBEOG66XBFN.
PhylomeDBP27250.
ProtClustDBCLSK880885.

Enzyme and pathway databases

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

Gene expression databases

GenevestigatorP27250.

Family and domain databases

Gene3D3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProIPR013149. ADH_C.
IPR013154. ADH_GroES-like.
IPR002085. ADH_SF_Zn-type.
IPR002328. ADH_Zn_CS.
IPR006140. D-isomer_2_OHA_DH_NAD-bd.
IPR011032. GroES-like.
IPR016040. NAD(P)-bd_dom.
[Graphical view]
PANTHERPTHR11695. PTHR11695. 1 hit.
PfamPF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view]
SUPFAMSSF50129. SSF50129. 1 hit.
PROSITEPS00059. ADH_ZINC. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

PROP27250.

Entry information

Entry nameAHR_ECOLI
AccessionPrimary (citable) accession number: P27250
Secondary accession number(s): P76812, Q2M640
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: February 1, 1995
Last modified: April 16, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Escherichia coli

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