AHR_ECOLI
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 03-AUG-2022, entry version 159.
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., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT 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., Mau B.,
RA 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 MG1655
RT 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., Hagen W.R.,
RA 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 aldehyde
RT 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 in
RT 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 corresponding
CC alcohols. Has a strong preference for NADPH over NADH as the electron
CC donor. Cannot use glyceraldehyde or a ketone as substrate. Is a
CC relevant source of NADPH-dependent aldehyde reductase activity in
CC E.coli. The in vivo functions of Ahr has yet to be determined.
CC {ECO:0000269|PubMed:22731523, ECO:0000269|PubMed:23093176,
CC 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; EC=1.1.1.2;
CC Evidence={ECO:0000269|PubMed:23093176, 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. {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 is
CC 312 sec(-1) for glutaraldehyde reduction. kcat is 2.6 sec(-1) for 5-
CC hydroxyvalerate reduction. kcat is 419 sec(-1) for hexanaldehyde
CC reduction. kcat is 313 sec(-1) for benzaldehyde reduction. kcat is
CC 224 sec(-1) for furfural reduction. kcat is 13.8 sec(-1) for butanol
CC oxidation. kcat is 12.9 sec(-1) for 1,4-butanediol oxidation.;
CC Temperature dependence:
CC Optimum temperature is 37-50 degrees Celsius using butyraldehyde as
CC substrate. {ECO:0000269|PubMed:23093176};
CC -!- BIOTECHNOLOGY: This enzyme can be applied to the microbial production
CC of fatty alcohols that have numerous applications as fuels, fragrances,
CC emollients, food additives, and detergents. Thus, together with
CC complementing enzymes, the broad substrate specificity of Ahr opens the
CC road for direct and tailored enzyme-catalyzed conversion of lipids into
CC user-ready chemical 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=Extended N-terminus.; Evidence={ECO:0000305};
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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 PDB; 7BU2; X-ray; 1.55 A; A/B=1-339.
DR PDBsum; 7BU2; -.
DR AlphaFoldDB; P27250; -.
DR SMR; P27250; -.
DR BioGRID; 4263049; 10.
DR STRING; 511145.b4269; -.
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 eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_6; -.
DR InParanoid; P27250; -.
DR OMA; FARNEHK; -.
DR PhylomeDB; P27250; -.
DR BioCyc; EcoCyc:EG11436-MON; -.
DR BioCyc; MetaCyc:EG11436-MON; -.
DR BRENDA; 1.1.1.183; 2026.
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:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IBA:GO_Central.
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-like_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 3D-structure; Fatty acid metabolism; Lipid metabolism; Metal-binding; NADP;
KW Oxidoreductase; Reference proteome; Zinc.
FT CHAIN 1..339
FT /note="Aldehyde reductase Ahr"
FT /id="PRO_0000160894"
FT BINDING 38
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 63
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 102
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 110
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT CONFLICT 331..339
FT /note="YRVVLKADF -> TAWC (in Ref. 1; AAA72122)"
FT /evidence="ECO:0000305"
FT STRAND 4..11
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 16..21
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 30..40
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 42..48
FT /evidence="ECO:0007829|PDB:7BU2"
FT TURN 49..52
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 57..59
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 86..89
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 91..94
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 100..103
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 117..120
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 123..131
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 132..134
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 135..137
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 144..147
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 148..151
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 153..163
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 171..175
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 179..190
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 194..200
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 207..211
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 214..218
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 222..226
FT /evidence="ECO:0007829|PDB:7BU2"
FT TURN 227..230
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 232..237
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 246..250
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 252..260
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 272..278
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 281..284
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 290..303
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 309..313
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 314..316
FT /evidence="ECO:0007829|PDB:7BU2"
FT HELIX 317..325
FT /evidence="ECO:0007829|PDB:7BU2"
FT STRAND 330..336
FT /evidence="ECO:0007829|PDB:7BU2"
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
