GenomeNet

Database: UniProt
Entry: P0A9Q7
LinkDB: P0A9Q7
Original site: P0A9Q7 
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   19-MAR-2014, entry version 80.
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 277:1453-1462(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       Self; NbExp=2; IntAct=EBI-543417, EBI-543417;
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_000913.3.
DR   RefSeq; YP_489507.1; NC_007779.1.
DR   ProteinModelPortal; P0A9Q7; -.
DR   SMR; P0A9Q7; 3-448, 450-864.
DR   BioGrid; 850204; 1.
DR   DIP; DIP-35790N; -.
DR   IntAct; P0A9Q7; 18.
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; WHKLPSS; -.
DR   OrthoDB; EOG6TFCQS; -.
DR   ProtClustDB; PRK13805; -.
DR   BioCyc; EcoCyc:ADHE-MONOMER; -.
DR   BioCyc; ECOL316407:JW1228-MONOMER; -.
DR   BioCyc; MetaCyc:ADHE-MONOMER; -.
DR   PRO; PR:P0A9Q7; -.
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; SSF53720; 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
//
DBGET integrated database retrieval system