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Database: UniProt
Entry: P27250
LinkDB: P27250
Original site: P27250 
ID   AHR_ECOLI               Reviewed;         339 AA.
AC   P27250; P76812; Q2M640;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 2.
DT   13-FEB-2019, entry version 143.
DE   RecName: Full=Aldehyde reductase Ahr;
DE            EC=1.1.1.2;
DE   AltName: Full=Zinc-dependent alcohol dehydrogenase Ahr;
GN   Name=ahr; Synonyms=yjgB; OrderedLocusNames=b4269, JW5761;
OS   Escherichia coli (strain K12).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B;
RA   Pucci M.J., Discotto L.F., Dougherty T.J.;
RL   Submitted (SEP-1992) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA   Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L.,
RA   Blattner F.R.;
RT   "Analysis of the Escherichia coli genome VI: DNA sequence of the
RT   region from 92.8 through 100 minutes.";
RL   Nucleic Acids Res. 23:2105-2119(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / MG1655 / ATCC 47076;
RX   PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA   Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA   Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA   Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
RA   Mau B., Shao Y.;
RT   "The complete genome sequence of Escherichia coli K-12.";
RL   Science 277:1453-1462(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=16738553; DOI=10.1038/msb4100049;
RA   Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA   Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT   "Highly accurate genome sequences of Escherichia coli K-12 strains
RT   MG1655 and W3110.";
RL   Mol. Syst. Biol. 2:E1-E5(2006).
RN   [5]
RP   IDENTIFICATION BY MASS SPECTROMETRY, ZINC-BINDING, AND COFACTOR.
RX   PubMed=22094925; DOI=10.1039/c1mt00154j;
RA   Sevcenco A.M., Pinkse M.W., Wolterbeek H.T., Verhaert P.D.,
RA   Hagen W.R., Hagedoorn P.L.;
RT   "Exploring the microbial metalloproteome using MIRAGE.";
RL   Metallomics 3:1324-1330(2011).
RN   [6]
RP   FUNCTION.
RX   PubMed=22731523; DOI=10.1186/1475-2859-11-90;
RA   Rodriguez G.M., Atsumi S.;
RT   "Isobutyraldehyde production from Escherichia coli by removing
RT   aldehyde reductase activity.";
RL   Microb. Cell Fact. 11:90-90(2012).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, CATALYTIC ACTIVITY,
RP   SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, AND 3D-STRUCTURE
RP   MODELING.
RC   STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX   PubMed=23093176; DOI=10.1007/s00253-012-4474-5;
RA   Pick A., Ruhmann B., Schmid J., Sieber V.;
RT   "Novel CAD-like enzymes from Escherichia coli K-12 as additional tools
RT   in chemical production.";
RL   Appl. Microbiol. Biotechnol. 97:5815-5824(2013).
RN   [8]
RP   FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, GENE NAME, AND
RP   BIOTECHNOLOGY.
RC   STRAIN=B / BL21-DE3;
RX   PubMed=23248280; DOI=10.1073/pnas.1216516110;
RA   Akhtar M.K., Turner N.J., Jones P.R.;
RT   "Carboxylic acid reductase is a versatile enzyme for the conversion of
RT   fatty acids into fuels and chemical commodities.";
RL   Proc. Natl. Acad. Sci. U.S.A. 110:87-92(2013).
CC   -!- FUNCTION: Catalyzes the reduction of a wide range of aldehydes
CC       including aliphatic fatty aldehydes (C4-C16), into their
CC       corresponding alcohols. Has a strong preference for NADPH over
CC       NADH as the electron donor. Cannot use glyceraldehyde or a ketone
CC       as substrate. Is a relevant source of NADPH-dependent aldehyde
CC       reductase activity in E.coli. The in vivo functions of Ahr has yet
CC       to be determined. {ECO:0000269|PubMed:22731523,
CC       ECO:0000269|PubMed:23093176, ECO:0000269|PubMed:23248280}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a primary alcohol + NADP(+) = an aldehyde + H(+) + NADPH;
CC         Xref=Rhea:RHEA:15937, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC         ChEBI:CHEBI:17478, ChEBI:CHEBI:57783, ChEBI:CHEBI:58349;
CC         EC=1.1.1.2; Evidence={ECO:0000269|PubMed:23093176,
CC         ECO:0000269|PubMed:23248280};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000305|PubMed:22094925};
CC       Note=Binds 2 Zn(2+) ions per subunit.
CC       {ECO:0000305|PubMed:22094925};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=73.4 mM for acetaldehyde {ECO:0000269|PubMed:23093176};
CC         KM=19.6 mM for propionaldehyde {ECO:0000269|PubMed:23093176};
CC         KM=2.1 mM for butyraldehyde {ECO:0000269|PubMed:23093176};
CC         KM=193.7 mM for isobutyraldehyde {ECO:0000269|PubMed:23093176};
CC         KM=2.4 mM for crotonaldehyde {ECO:0000269|PubMed:23093176};
CC         KM=5.8 mM for glutaraldehyde {ECO:0000269|PubMed:23093176};
CC         KM=59.7 mM for 5-hydroxyvalerate {ECO:0000269|PubMed:23093176};
CC         KM=0.34 mM for hexanaldehyde {ECO:0000269|PubMed:23093176};
CC         KM=0.24 mM for benzaldehyde {ECO:0000269|PubMed:23093176};
CC         KM=0.22 mM for furfural {ECO:0000269|PubMed:23093176};
CC         KM=3.5 mM for butanol {ECO:0000269|PubMed:23093176};
CC         KM=24.1 mM for 1,4-butanediol {ECO:0000269|PubMed:23093176};
CC         KM=0.06 mM for NADPH {ECO:0000269|PubMed:23093176};
CC         KM=0.076 mM for NADP(+) {ECO:0000269|PubMed:23093176};
CC         Note=kcat is 333 sec(-1) for acetaldehyde reduction. kcat is 207
CC         sec(-1) for propionaldehyde reduction. kcat is 464 sec(-1) for
CC         butyraldehyde reduction. kcat is 51 sec(-1) for isobutyraldehyde
CC         reduction. kcat is 78 sec(-1) for crotonaldehyde reduction. kcat
CC         is 312 sec(-1) for glutaraldehyde reduction. kcat is 2.6 sec(-1)
CC         for 5-hydroxyvalerate reduction. kcat is 419 sec(-1) for
CC         hexanaldehyde reduction. kcat is 313 sec(-1) for benzaldehyde
CC         reduction. kcat is 224 sec(-1) for furfural reduction. kcat is
CC         13.8 sec(-1) for butanol oxidation. kcat is 12.9 sec(-1) for
CC         1,4-butanediol oxidation.;
CC       Temperature dependence:
CC         Optimum temperature is 37-50 degrees Celsius using butyraldehyde
CC         as substrate. {ECO:0000269|PubMed:23093176};
CC   -!- BIOTECHNOLOGY: This enzyme can be applied to the microbial
CC       production of fatty alcohols that have numerous applications as
CC       fuels, fragrances, emollients, food additives, and detergents.
CC       Thus, together with complementing enzymes, the broad substrate
CC       specificity of Ahr opens the road for direct and tailored enzyme-
CC       catalyzed conversion of lipids into user-ready chemical
CC       commodities. {ECO:0000269|PubMed:23248280}.
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA97166.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
DR   EMBL; M96355; AAA72122.1; -; Genomic_DNA.
DR   EMBL; U14003; AAA97166.1; ALT_INIT; Genomic_DNA.
DR   EMBL; U00096; AAC77226.2; -; Genomic_DNA.
DR   EMBL; AP009048; BAE78266.1; -; Genomic_DNA.
DR   PIR; S56495; S56495.
DR   RefSeq; NP_418690.4; NC_000913.3.
DR   RefSeq; WP_001309160.1; NZ_LN832404.1.
DR   ProteinModelPortal; P27250; -.
DR   SMR; P27250; -.
DR   BioGrid; 4263049; 10.
DR   STRING; 316385.ECDH10B_4462; -.
DR   jPOST; P27250; -.
DR   PaxDb; P27250; -.
DR   PRIDE; P27250; -.
DR   EnsemblBacteria; AAC77226; AAC77226; b4269.
DR   EnsemblBacteria; BAE78266; BAE78266; BAE78266.
DR   GeneID; 948802; -.
DR   KEGG; ecj:JW5761; -.
DR   KEGG; eco:b4269; -.
DR   PATRIC; fig|511145.12.peg.4400; -.
DR   EchoBASE; EB1406; -.
DR   EcoGene; EG11436; ahr.
DR   eggNOG; ENOG4105DQ4; Bacteria.
DR   eggNOG; COG1064; LUCA.
DR   HOGENOM; HOG000294667; -.
DR   InParanoid; P27250; -.
DR   KO; K12957; -.
DR   PhylomeDB; P27250; -.
DR   BioCyc; EcoCyc:EG11436-MONOMER; -.
DR   BioCyc; ECOL316407:JW5761-MONOMER; -.
DR   BioCyc; MetaCyc:EG11436-MONOMER; -.
DR   PRO; PR:P27250; -.
DR   Proteomes; UP000000318; Chromosome.
DR   Proteomes; UP000000625; Chromosome.
DR   GO; GO:0008106; F:alcohol dehydrogenase (NADP+) activity; IDA:EcoCyc.
DR   GO; GO:0008270; F:zinc ion binding; IDA:EcoCyc.
DR   GO; GO:0006631; P:fatty acid metabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013149; ADH_C.
DR   InterPro; IPR013154; ADH_N.
DR   InterPro; IPR002328; ADH_Zn_CS.
DR   InterPro; IPR029752; D-isomer_DH_CS1.
DR   InterPro; IPR011032; GroES-like_sf.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR020843; PKS_ER.
DR   Pfam; PF08240; ADH_N; 1.
DR   Pfam; PF00107; ADH_zinc_N; 1.
DR   SMART; SM00829; PKS_ER; 1.
DR   SUPFAM; SSF50129; SSF50129; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
DR   PROSITE; PS00059; ADH_ZINC; 1.
PE   1: Evidence at protein level;
KW   Complete proteome; Fatty acid metabolism; Lipid metabolism;
KW   Metal-binding; NADP; Oxidoreductase; Reference proteome; Zinc.
FT   CHAIN         1    339       Aldehyde reductase Ahr.
FT                                /FTId=PRO_0000160894.
FT   METAL        38     38       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        63     63       Zinc 1; catalytic. {ECO:0000250}.
FT   METAL        96     96       Zinc 2. {ECO:0000250}.
FT   METAL        99     99       Zinc 2. {ECO:0000250}.
FT   METAL       102    102       Zinc 2. {ECO:0000250}.
FT   METAL       110    110       Zinc 2. {ECO:0000250}.
FT   METAL       152    152       Zinc 1; catalytic. {ECO:0000250}.
FT   CONFLICT    331    339       YRVVLKADF -> TAWC (in Ref. 1; AAA72122).
FT                                {ECO:0000305}.
SQ   SEQUENCE   339 AA;  36502 MW;  0854DDEFA16B9EEE CRC64;
     MSMIKSYAAK EAGGELEVYE YDPGELRPQD VEVQVDYCGI CHSDLSMIDN EWGFSQYPLV
     AGHEVIGRVV ALGSAAQDKG LQVGQRVGIG WTARSCGHCD ACISGNQINC EQGAVPTIMN
     RGGFAEKLRA DWQWVIPLPE NIDIESAGPL LCGGITVFKP LLMHHITATS RVGVIGIGGL
     GHIAIKLLHA MGCEVTAFSS NPAKEQEVLA MGADKVVNSR DPQALKALAG QFDLIINTVN
     VSLDWQPYFE ALTYGGNFHT VGAVLTPLSV PAFTLIAGDR SVSGSATGTP YELRKLMRFA
     ARSKVAPTTE LFPMSKINDA IQHVRDGKAR YRVVLKADF
//
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