ID   ADHE_ECO57              Reviewed;         891 AA.
AC   P0A9Q8; P17547;
DT   19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   16-JUN-2009, entry version 27.
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; OrderedLocusNames=Z2016, ECs1741;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   MEDLINE=21074935; PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   MEDLINE=21156231; PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
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 (By similarity).
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 (By similarity).
CC   -!- SUBUNIT: Seems to form a rod shaped polymer composed of about 40
CC       identical subunits (By similarity).
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.
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DR   EMBL; AE005174; AAG56096.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB35164.1; -; Genomic_DNA.
DR   PIR; E90846; E90846.
DR   RefSeq; NP_287484.1; -.
DR   RefSeq; NP_309768.1; -.
DR   GeneID; 913110; -.
DR   GeneID; 960491; -.
DR   GenomeReviews; AE005174_GR; Z2016.
DR   GenomeReviews; BA000007_GR; ECs1741.
DR   KEGG; ece:Z2016; -.
DR   KEGG; ecs:ECs1741; -.
DR   HOGENOM; P0A9Q8; -.
DR   BioCyc; ECOL83334:ECS1741-MON; -.
DR   GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) ac...; IEA:EC.
DR   GO; GO:0004022; F:alcohol dehydrogenase activity; IEA:EC.
DR   GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR   GO; GO:0006066; P:cellular alcohol metabolic process; IEA:InterPro.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR001670; ADH_Fe.
DR   InterPro; IPR018211; ADH_Fe_CS.
DR   InterPro; IPR015590; Aldehyde_DH.
DR   InterPro; IPR012079; Bifunc_Ald/AlcDH.
DR   Pfam; PF00171; Aldedh; 1.
DR   Pfam; PF00465; Fe-ADH; 1.
DR   PIRSF; PIRSF000111; ALDH_ADH; 1.
DR   PROSITE; PS00913; ADH_IRON_1; 1.
DR   PROSITE; PS00060; ADH_IRON_2; 1.
PE   3: Inferred from homology;
KW   Acetylation; Complete proteome; Iron; Multifunctional enzyme; NAD;
KW   Oxidoreductase.
FT   INIT_MET      1      1       Removed (By similarity).
FT   CHAIN         2    891       Aldehyde-alcohol dehydrogenase.
FT                                /FTId=PRO_0000087838.
FT   NP_BIND     422    427       NAD (Potential).
FT   ACT_SITE    246    246       By similarity.
FT   MOD_RES     358    358       N6-acetyllysine (By similarity).
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
//