ID ADHE_ECOLI Reviewed; 891 AA.
AC P0A9Q7; P17547;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 01-MAY-2013, entry version 75.
DE RecName: Full=Aldehyde-alcohol dehydrogenase;
DE Includes:
DE RecName: Full=Alcohol dehydrogenase;
DE Short=ADH;
DE EC=1.1.1.1;
DE Includes:
DE RecName: Full=Acetaldehyde dehydrogenase [acetylating];
DE Short=ACDH;
DE EC=1.2.1.10;
DE Includes:
DE RecName: Full=Pyruvate-formate-lyase deactivase;
DE Short=PFL deactivase;
GN Name=adhE; Synonyms=ana; OrderedLocusNames=b1241, JW1228;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=2695398; DOI=10.1016/0378-1119(89)90483-6;
RA Goodlove P.E., Cunningham P.R., Parker J., Clark D.P.;
RT "Cloning and sequence analysis of the fermentative alcohol-
RT dehydrogenase-encoding gene of Escherichia coli.";
RL Gene 85:209-214(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, AND
RP CHARACTERIZATION.
RC STRAIN=K12;
RX PubMed=2015910; DOI=10.1016/0014-5793(91)80358-A;
RA Kessler D., Leibrecht I., Knappe J.;
RT "Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities
RT of Escherichia coli reside on a polymeric protein particle encoded by
RT adhE.";
RL FEBS Lett. 281:59-63(1991).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A.,
RA Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA Yano M., Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT corresponding to the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [4]
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 277:1453-1474(1997).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 849-891.
RC STRAIN=K12;
RX PubMed=7773397;
RA Danchin A., Krin E.;
RT "Filling the gap between hns and adhE in Escherichia coli K12.";
RL Microbiology 141:959-960(1995).
RN [7]
RP PROTEIN SEQUENCE OF 2-21.
RX PubMed=7521508;
RA Yamato M., Takahashi Y., Tomotake H., Ota F., Hirota K., Yamaguchi K.;
RT "Monoclonal antibodies to spirosin of Yersinia enterocolitica and
RT analysis of the localization of spirosome by use of them.";
RL Microbiol. Immunol. 38:177-182(1994).
RN [8]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R.,
RA Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [9]
RP ANTIOXIDANT ROLE OF ADHE.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=12783863; DOI=10.1074/jbc.M304351200;
RA Echave P., Tamarit J., Cabiscol E., Ros J.;
RT "Novel antioxidant role of alcohol dehydrogenase E from Escherichia
RT coli.";
RL J. Biol. Chem. 278:30193-30198(2003).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-358, AND MASS SPECTROMETRY.
RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076;
RX PubMed=18723842; DOI=10.1074/mcp.M800187-MCP200;
RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F.,
RA Grishin N.V., Zhao Y.;
RT "Lysine acetylation is a highly abundant and evolutionarily conserved
RT modification in Escherichia coli.";
RL Mol. Cell. Proteomics 8:215-225(2009).
CC -!- FUNCTION: This enzyme has three activities: ADH, ACDH, and PFL-
CC deactivase. In aerobic conditions it acts as a hydrogen peroxide
CC scavenger. The PFL deactivase activity catalyzes the quenching of
CC the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA
CC dependent reaction.
CC -!- CATALYTIC ACTIVITY: An alcohol + NAD(+) = an aldehyde or ketone +
CC NADH.
CC -!- CATALYTIC ACTIVITY: Acetaldehyde + CoA + NAD(+) = acetyl-CoA +
CC NADH.
CC -!- COFACTOR: Iron.
CC -!- SUBUNIT: Seems to form a rod shaped polymer composed of about 40
CC identical subunits.
CC -!- INTERACTION:
CC P0A7V0:rpsB; NbExp=1; IntAct=EBI-543417, EBI-543439;
CC -!- INDUCTION: Under anaerobic conditions in the absence of nitrate.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family.
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-
CC containing alcohol dehydrogenase family.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs License
CC -----------------------------------------------------------------------
DR EMBL; X59263; CAA41955.1; -; Genomic_DNA.
DR EMBL; M33504; AAA23420.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74323.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA36121.1; -; Genomic_DNA.
DR EMBL; X67326; CAA47743.1; -; Genomic_DNA.
DR PIR; JS0406; DEEC.
DR RefSeq; NP_415757.1; NC_000913.2.
DR RefSeq; YP_489507.1; NC_007779.1.
DR ProteinModelPortal; P0A9Q7; -.
DR SMR; P0A9Q7; 3-448, 465-862.
DR DIP; DIP-35790N; -.
DR IntAct; P0A9Q7; 17.
DR MINT; MINT-1288364; -.
DR STRING; 511145.b1241; -.
DR PaxDb; P0A9Q7; -.
DR PRIDE; P0A9Q7; -.
DR EnsemblBacteria; AAC74323; AAC74323; b1241.
DR EnsemblBacteria; BAA36121; BAA36121; BAA36121.
DR GeneID; 12930611; -.
DR GeneID; 945837; -.
DR KEGG; ecj:Y75_p1213; -.
DR KEGG; eco:b1241; -.
DR PATRIC; 32117740; VBIEscCol129921_1290.
DR EchoBASE; EB0030; -.
DR EcoGene; EG10031; adhE.
DR eggNOG; COG1012; -.
DR HOGENOM; HOG000025256; -.
DR KO; K04072; -.
DR OMA; YVSVMAN; -.
DR ProtClustDB; PRK13805; -.
DR BioCyc; EcoCyc:ADHE-MONOMER; -.
DR BioCyc; ECOL316407:JW1228-MONOMER; -.
DR BioCyc; MetaCyc:ADHE-MONOMER; -.
DR Genevestigator; P0A9Q7; -.
DR GO; GO:0005829; C:cytosol; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IMP:EcoliWiki.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD) activity; IMP:EcoliWiki.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR GO; GO:0006115; P:ethanol biosynthetic process; IDA:EcoliWiki.
DR Gene3D; 3.40.309.10; -; 2.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR001670; ADH_Fe.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR016161; Ald_DH/histidinol_DH.
DR InterPro; IPR016163; Ald_DH_C.
DR InterPro; IPR016162; Ald_DH_N.
DR InterPro; IPR015590; Aldehyde_DH_dom.
DR InterPro; IPR012079; Bifunc_Ald/ADH.
DR Pfam; PF00171; Aldedh; 1.
DR Pfam; PF00465; Fe-ADH; 1.
DR PIRSF; PIRSF000111; ALDH_ADH; 1.
DR SUPFAM; SSF53720; Aldehyde_DH/Histidinol_DH; 1.
DR PROSITE; PS00913; ADH_IRON_1; 1.
DR PROSITE; PS00060; ADH_IRON_2; 1.
PE 1: Evidence at protein level;
KW Acetylation; Complete proteome; Direct protein sequencing; Iron;
KW Multifunctional enzyme; NAD; Oxidoreductase; Reference proteome.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 891 Aldehyde-alcohol dehydrogenase.
FT /FTId=PRO_0000087837.
FT NP_BIND 422 427 NAD (Potential).
FT ACT_SITE 246 246 By similarity.
FT MOD_RES 358 358 N6-acetyllysine.
SQ SEQUENCE 891 AA; 96127 MW; 75469F57419C8C79 CRC64;
MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG
IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA
IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA
LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF
DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP
AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV
AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG
CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK
RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI
IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME
AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG
VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD
HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ
CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A
//
