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Database: UniProt
Entry: P75691
LinkDB: P75691
Original site: P75691 
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   13-FEB-2019, entry version 150.
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.,
RA   Mau B., 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
RT   MG1655 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.,
RA   Hagen W.R., 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,
RP   AND 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
RT   in 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
CC       into their corresponding alcohols. Has a strong preference for
CC       NADPH over NADH as the electron donor. Cannot use a ketone as
CC       substrate. Is a major source of NADPH-dependent aldehyde reductase
CC       activity in E.coli. The in vivo functions of YahK has yet to be
CC       determined. {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;
CC         EC=1.1.1.2; 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.
CC       {ECO:0000269|PubMed:22094925, 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
CC         11.6 sec(-1) for propionaldehyde reduction. kcat is 12.3 sec(-1)
CC         for glyceraldehyde reduction. kcat is 41.6 sec(-1) for
CC         butyraldehyde reduction. kcat is 32.1 sec(-1) for
CC         isobutyraldehyde reduction. kcat is 32.6 sec(-1) for
CC         crotonaldehyde reduction. kcat is 13.4 sec(-1) for
CC         glutaraldehyde reduction. kcat is 0.18 sec(-1) for 5-
CC         hydroxyvalerate reduction. kcat is 18.3 sec(-1) for
CC         hexanaldehyde reduction. kcat is 7.75 sec(-1) for benzaldehyde
CC         reduction. kcat is 12.5 sec(-1) for furfural reduction. kcat is
CC         4.7 sec(-1) for butanol oxidation. kcat is 6.7 sec(-1) for 1,4-
CC         butanediol oxidation.;
CC       Temperature dependence:
CC         Shows a constant increase in activity until 60 degrees Celsius
CC         using butyraldehyde as substrate. {ECO:0000269|PubMed:23093176};
CC   -!- SIMILARITY: Belongs to the zinc-containing alcohol dehydrogenase
CC       family. {ECO:0000305}.
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_LN832404.1.
DR   PDB; 1UUF; X-ray; 1.76 A; A=2-349.
DR   PDBsum; 1UUF; -.
DR   ProteinModelPortal; P75691; -.
DR   SMR; P75691; -.
DR   BioGrid; 4259802; 7.
DR   DIP; DIP-11263N; -.
DR   IntAct; P75691; 10.
DR   STRING; 316407.85674468; -.
DR   SWISS-2DPAGE; P75691; -.
DR   EPD; 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   EcoGene; EG13595; yahK.
DR   eggNOG; ENOG4105DQ4; Bacteria.
DR   eggNOG; COG1064; LUCA.
DR   HOGENOM; HOG000294667; -.
DR   InParanoid; P75691; -.
DR   KO; K13979; -.
DR   PhylomeDB; P75691; -.
DR   BioCyc; EcoCyc:G6190-MONOMER; -.
DR   BioCyc; ECOL316407:JW0317-MONOMER; -.
DR   BioCyc; MetaCyc:G6190-MONOMER; -.
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:0008270; F:zinc ion binding; IEA:InterPro.
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   3D-structure; Complete proteome; Metal-binding; NADP; Oxidoreductase;
KW   Reference proteome; Zinc.
FT   CHAIN         1    349       Aldehyde reductase YahK.
FT                                /FTId=PRO_0000160888.
FT   METAL        40     40       Zinc 1; catalytic.
FT   METAL        62     62       Zinc 1; catalytic.
FT   METAL        93     93       Zinc 2.
FT   METAL        96     96       Zinc 2.
FT   METAL        99     99       Zinc 2.
FT   METAL       107    107       Zinc 2.
FT   METAL       158    158       Zinc 1; catalytic.
FT   CONFLICT    116    116       S -> L (in Ref. 1; AAB18051).
FT                                {ECO:0000305}.
FT   CONFLICT    145    145       H -> Y (in Ref. 1; AAB18051).
FT                                {ECO:0000305}.
FT   STRAND        4     10       {ECO:0000244|PDB:1UUF}.
FT   STRAND       16     19       {ECO:0000244|PDB:1UUF}.
FT   STRAND       29     38       {ECO:0000244|PDB:1UUF}.
FT   HELIX        41     48       {ECO:0000244|PDB:1UUF}.
FT   STRAND       56     58       {ECO:0000244|PDB:1UUF}.
FT   STRAND       64     71       {ECO:0000244|PDB:1UUF}.
FT   STRAND       83     86       {ECO:0000244|PDB:1UUF}.
FT   STRAND       88     91       {ECO:0000244|PDB:1UUF}.
FT   STRAND       94     96       {ECO:0000244|PDB:1UUF}.
FT   HELIX        97    100       {ECO:0000244|PDB:1UUF}.
FT   HELIX       104    106       {ECO:0000244|PDB:1UUF}.
FT   TURN        113    115       {ECO:0000244|PDB:1UUF}.
FT   STRAND      128    136       {ECO:0000244|PDB:1UUF}.
FT   HELIX       137    139       {ECO:0000244|PDB:1UUF}.
FT   HELIX       147    149       {ECO:0000244|PDB:1UUF}.
FT   HELIX       150    153       {ECO:0000244|PDB:1UUF}.
FT   HELIX       154    157       {ECO:0000244|PDB:1UUF}.
FT   HELIX       159    169       {ECO:0000244|PDB:1UUF}.
FT   STRAND      177    181       {ECO:0000244|PDB:1UUF}.
FT   HELIX       185    196       {ECO:0000244|PDB:1UUF}.
FT   STRAND      200    207       {ECO:0000244|PDB:1UUF}.
FT   HELIX       208    210       {ECO:0000244|PDB:1UUF}.
FT   HELIX       211    217       {ECO:0000244|PDB:1UUF}.
FT   STRAND      220    224       {ECO:0000244|PDB:1UUF}.
FT   HELIX       228    232       {ECO:0000244|PDB:1UUF}.
FT   TURN        233    236       {ECO:0000244|PDB:1UUF}.
FT   STRAND      238    243       {ECO:0000244|PDB:1UUF}.
FT   HELIX       251    255       {ECO:0000244|PDB:1UUF}.
FT   STRAND      258    266       {ECO:0000244|PDB:1UUF}.
FT   HELIX       279    283       {ECO:0000244|PDB:1UUF}.
FT   TURN        284    286       {ECO:0000244|PDB:1UUF}.
FT   STRAND      288    291       {ECO:0000244|PDB:1UUF}.
FT   HELIX       297    310       {ECO:0000244|PDB:1UUF}.
FT   STRAND      316    319       {ECO:0000244|PDB:1UUF}.
FT   HELIX       321    323       {ECO:0000244|PDB:1UUF}.
FT   HELIX       324    332       {ECO:0000244|PDB:1UUF}.
FT   STRAND      336    343       {ECO:0000244|PDB:1UUF}.
FT   HELIX       344    347       {ECO:0000244|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
//
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