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P27250

- AHR_ECOLI

UniProt

P27250 - AHR_ECOLI

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Protein

Aldehyde reductase Ahr

Gene

ahr

Organism
Escherichia coli (strain K12)
Status
Reviewed - 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

Binds 2 zinc 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

  1. alcohol dehydrogenase (NADP+) activity Source: EcoCyc
  2. zinc ion binding Source: EcoCyc

GO - Biological processi

  1. fatty acid metabolic process Source: UniProtKB-KW
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: Chromosome, UP000000625: 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.
OMAiPMSKINE.
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.

Experimental Info

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
YP_492407.1. NC_007779.1.

Genome annotation databases

EnsemblBacteriaiAAC77226; AAC77226; b4269.
BAE78266; BAE78266; BAE78266.
GeneIDi12934055.
948802.
KEGGiecj:Y75_p4152.
eco:b4269.
PATRICi32124111. VBIEscCol129921_4400.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
PIRi S56495.
RefSeqi NP_418690.4. NC_000913.3.
YP_492407.1. NC_007779.1.

3D structure databases

ProteinModelPortali P27250.
SMRi P27250. Positions 7-335.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 511145.b4269.

Proteomic databases

PaxDbi P27250.
PRIDEi P27250.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAC77226 ; AAC77226 ; b4269 .
BAE78266 ; BAE78266 ; BAE78266 .
GeneIDi 12934055.
948802.
KEGGi ecj:Y75_p4152.
eco:b4269.
PATRICi 32124111. VBIEscCol129921_4400.

Organism-specific databases

EchoBASEi EB1406.
EcoGenei EG11436. ahr.

Phylogenomic databases

eggNOGi COG1064.
HOGENOMi HOG000294667.
InParanoidi P27250.
KOi K12957.
OMAi PMSKINE.
OrthoDBi EOG66XBFN.
PhylomeDBi P27250.

Enzyme and pathway databases

BioCyci EcoCyc:EG11436-MONOMER.
ECOL316407:JW5761-MONOMER.
MetaCyc:EG11436-MONOMER.

Miscellaneous databases

PROi P27250.

Gene expression databases

Genevestigatori P27250.

Family and domain databases

Gene3Di 3.40.50.720. 1 hit.
3.90.180.10. 1 hit.
InterProi IPR013149. 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 ]
PANTHERi PTHR11695. PTHR11695. 1 hit.
Pfami PF08240. ADH_N. 1 hit.
PF00107. ADH_zinc_N. 1 hit.
[Graphical view ]
SUPFAMi SSF50129. SSF50129. 1 hit.
PROSITEi PS00059. ADH_ZINC. 1 hit.
[Graphical view ]
ProtoNeti Search...

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: October 29, 2014
This is version 115 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