YAHK_ECOLI
ID YAHK_ECOLI Reviewed; 349 AA.
AC P75691; P71306; Q2MC98;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 168.
DE RecName: Full=Aldehyde reductase YahK;
DE EC=1.1.1.2;
DE AltName: Full=Zinc-dependent alcohol dehydrogenase YahK;
GN Name=yahK; OrderedLocusNames=b0325, JW0317;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [3]
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 [4]
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 [5]
RP IDENTIFICATION, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
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 [6]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ZINC IONS, AND
RP COFACTOR.
RA Jeudy S., Claverie J.-M., Abergel C.;
RT "Crystal structure of yahK, a zinc-type alcohol dehydrogenase-like
RT protein.";
RL Submitted (DEC-2003) to the PDB data bank.
CC -!- FUNCTION: Catalyzes the reduction of a wide range of aldehydes into
CC their corresponding alcohols. Has a strong preference for NADPH over
CC NADH as the electron donor. Cannot use a ketone as substrate. Is a
CC major source of NADPH-dependent aldehyde reductase activity in E.coli.
CC The in vivo functions of YahK has yet to be determined.
CC {ECO:0000269|PubMed:23093176}.
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};
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:22094925, ECO:0000269|Ref.6};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:22094925,
CC ECO:0000269|Ref.6};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=13.3 mM for acetaldehyde {ECO:0000269|PubMed:23093176};
CC KM=10.9 mM for propionaldehyde {ECO:0000269|PubMed:23093176};
CC KM=4.4 mM for glyceraldehyde {ECO:0000269|PubMed:23093176};
CC KM=2.1 mM for butyraldehyde {ECO:0000269|PubMed:23093176};
CC KM=2.2 mM for isobutyraldehyde {ECO:0000269|PubMed:23093176};
CC KM=3.6 mM for crotonaldehyde {ECO:0000269|PubMed:23093176};
CC KM=4.1 mM for glutaraldehyde {ECO:0000269|PubMed:23093176};
CC KM=52.6 mM for 5-hydroxyvalerate {ECO:0000269|PubMed:23093176};
CC KM=0.37 mM for hexanaldehyde {ECO:0000269|PubMed:23093176};
CC KM=0.29 mM for benzaldehyde {ECO:0000269|PubMed:23093176};
CC KM=0.135 mM for furfural {ECO:0000269|PubMed:23093176};
CC KM=6.6 mM for butanol {ECO:0000269|PubMed:23093176};
CC KM=38.5 mM for 1,4-butanediol {ECO:0000269|PubMed:23093176};
CC KM=0.011 mM for NADPH {ECO:0000269|PubMed:23093176};
CC KM=0.012 mM for NADP(+) {ECO:0000269|PubMed:23093176};
CC Note=kcat is 11.2 sec(-1) for acetaldehyde reduction. kcat is 11.6
CC sec(-1) for propionaldehyde reduction. kcat is 12.3 sec(-1) for
CC glyceraldehyde reduction. kcat is 41.6 sec(-1) for butyraldehyde
CC reduction. kcat is 32.1 sec(-1) for isobutyraldehyde reduction. kcat
CC is 32.6 sec(-1) for crotonaldehyde reduction. kcat is 13.4 sec(-1)
CC for glutaraldehyde reduction. kcat is 0.18 sec(-1) for 5-
CC hydroxyvalerate reduction. kcat is 18.3 sec(-1) for hexanaldehyde
CC reduction. kcat is 7.75 sec(-1) for benzaldehyde reduction. kcat is
CC 12.5 sec(-1) for furfural reduction. kcat is 4.7 sec(-1) for butanol
CC oxidation. kcat is 6.7 sec(-1) for 1,4-butanediol oxidation.;
CC Temperature dependence:
CC Shows a constant increase in activity until 60 degrees Celsius using
CC butyraldehyde as substrate. {ECO:0000269|PubMed:23093176};
CC -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC family. {ECO:0000305}.
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DR EMBL; U73857; AAB18051.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73428.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76108.1; -; Genomic_DNA.
DR PIR; E64759; E64759.
DR RefSeq; NP_414859.1; NC_000913.3.
DR RefSeq; WP_000692754.1; NZ_SSZK01000063.1.
DR PDB; 1UUF; X-ray; 1.76 A; A=2-349.
DR PDBsum; 1UUF; -.
DR AlphaFoldDB; P75691; -.
DR SMR; P75691; -.
DR BioGRID; 4259802; 7.
DR BioGRID; 849372; 2.
DR DIP; DIP-11263N; -.
DR IntAct; P75691; 10.
DR STRING; 511145.b0325; -.
DR SWISS-2DPAGE; P75691; -.
DR jPOST; P75691; -.
DR PaxDb; P75691; -.
DR PRIDE; P75691; -.
DR EnsemblBacteria; AAC73428; AAC73428; b0325.
DR EnsemblBacteria; BAE76108; BAE76108; BAE76108.
DR GeneID; 944975; -.
DR KEGG; ecj:JW0317; -.
DR KEGG; eco:b0325; -.
DR PATRIC; fig|1411691.4.peg.1952; -.
DR EchoBASE; EB3364; -.
DR eggNOG; COG1064; Bacteria.
DR HOGENOM; CLU_026673_20_2_6; -.
DR InParanoid; P75691; -.
DR OMA; YRFSIDM; -.
DR PhylomeDB; P75691; -.
DR BioCyc; EcoCyc:G6190-MON; -.
DR BioCyc; MetaCyc:G6190-MON; -.
DR EvolutionaryTrace; P75691; -.
DR PRO; PR:P75691; -.
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; IEA:InterPro.
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; Metal-binding; NADP; Oxidoreductase; Reference proteome;
KW Zinc.
FT CHAIN 1..349
FT /note="Aldehyde reductase YahK"
FT /id="PRO_0000160888"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 62
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT BINDING 93
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 96
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 99
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 107
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT BINDING 158
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT CONFLICT 116
FT /note="S -> L (in Ref. 1; AAB18051)"
FT /evidence="ECO:0000305"
FT CONFLICT 145
FT /note="H -> Y (in Ref. 1; AAB18051)"
FT /evidence="ECO:0000305"
FT STRAND 4..10
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 16..19
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 29..38
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 41..48
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 56..58
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 64..71
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 94..96
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 97..100
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 104..106
FT /evidence="ECO:0007829|PDB:1UUF"
FT TURN 113..115
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 128..136
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 137..139
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 150..153
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 154..157
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 177..181
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 185..196
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 200..207
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 208..210
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 211..217
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 220..224
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 228..232
FT /evidence="ECO:0007829|PDB:1UUF"
FT TURN 233..236
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 251..255
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 258..266
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 279..283
FT /evidence="ECO:0007829|PDB:1UUF"
FT TURN 284..286
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 297..310
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 316..319
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 321..323
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 324..332
FT /evidence="ECO:0007829|PDB:1UUF"
FT STRAND 336..343
FT /evidence="ECO:0007829|PDB:1UUF"
FT HELIX 344..347
FT /evidence="ECO:0007829|PDB:1UUF"
SQ SEQUENCE 349 AA; 37978 MW; AD0E2DF4D43C9B09 CRC64;
MKIKAVGAYS AKQPLEPMDI TRREPGPNDV KIEIAYCGVC HSDLHQVRSE WAGTVYPCVP
GHEIVGRVVA VGDQVEKYAP GDLVGVGCIV DSCKHCEECE DGLENYCDHM TGTYNSPTPD
EPGHTLGGYS QQIVVHERYV LRIRHPQEQL AAVAPLLCAG ITTYSPLRHW QAGPGKKVGV
VGIGGLGHMG IKLAHAMGAH VVAFTTSEAK REAAKALGAD EVVNSRNADE MAAHLKSFDF
ILNTVAAPHN LDDFTTLLKR DGTMTLVGAP ATPHKSPEVF NLIMKRRAIA GSMIGGIPET
QEMLDFCAEH GIVADIEMIR ADQINEAYER MLRGDVKYRF VIDNRTLTD
