ADHE_ECO57
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 03-AUG-2022, entry version 105.
DE RecName: Full=Bifunctional aldehyde-alcohol dehydrogenase AdhE {ECO:0000305};
DE AltName: Full=Alcohol dehydrogenase E {ECO:0000305};
DE Includes:
DE RecName: Full=Acetaldehyde dehydrogenase [acetylating] {ECO:0000305};
DE Short=ACDH {ECO:0000250|UniProtKB:P0A9Q7};
DE EC=1.2.1.10 {ECO:0000250|UniProtKB:P0A9Q7};
DE Includes:
DE RecName: Full=Alcohol dehydrogenase {ECO:0000303|PubMed:24846743};
DE Short=ADH {ECO:0000250|UniProtKB:P0A9Q7};
DE EC=1.1.1.1 {ECO:0000250|UniProtKB:P0A9Q7};
GN Name=adhE {ECO:0000303|PubMed:24846743}; OrderedLocusNames=Z2016, ECs1741;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
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 PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA 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 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., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
RN [3]
RP FUNCTION IN VIRULENCE, AND DISRUPTION PHENOTYPE.
RC STRAIN=O157:H7 / EHEC;
RX PubMed=24846743; DOI=10.1111/mmi.12651;
RA Beckham K.S., Connolly J.P., Ritchie J.M., Wang D., Gawthorne J.A.,
RA Tahoun A., Gally D.L., Burgess K., Burchmore R.J., Smith B.O.,
RA Beatson S.A., Byron O., Wolfe A.J., Douce G.R., Roe A.J.;
RT "The metabolic enzyme AdhE controls the virulence of Escherichia coli
RT O157:H7.";
RL Mol. Microbiol. 93:199-211(2014).
RN [4] {ECO:0007744|PDB:6SCG, ECO:0007744|PDB:6SCI}
RP X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 451-891 IN COMPLEXES WITH NAD AND
RP IRON, AND COFACTOR.
RC STRAIN=O157:H7 / EHEC;
RX PubMed=32880589; DOI=10.1107/s2053230x20010237;
RA Azmi L., Bragginton E.C., Cadby I.T., Byron O., Roe A.J., Lovering A.L.,
RA Gabrielsen M.;
RT "High-resolution structure of the alcohol dehydrogenase domain of the
RT bifunctional bacterial enzyme AdhE.";
RL Acta Crystallogr. F Struct. Biol. Commun. 76:414-421(2020).
CC -!- FUNCTION: Under fermentative conditions, catalyzes the sequential NADH-
CC dependent reduction of acetyl-CoA to acetaldehyde and then to ethanol
CC (By similarity). Plays an important role in virulence and is critical
CC for proper regulation of virulence gene expression (PubMed:24846743).
CC {ECO:0000250|UniProtKB:P0A9Q7, ECO:0000269|PubMed:24846743}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=acetaldehyde + CoA + NAD(+) = acetyl-CoA + H(+) + NADH;
CC Xref=Rhea:RHEA:23288, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:57287, ChEBI:CHEBI:57288, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.2.1.10;
CC Evidence={ECO:0000250|UniProtKB:P0A9Q7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:23290;
CC Evidence={ECO:0000250|UniProtKB:P0A9Q7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ethanol + NAD(+) = acetaldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:25290, ChEBI:CHEBI:15343, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16236, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P0A9Q7};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:25292;
CC Evidence={ECO:0000250|UniProtKB:P0A9Q7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a primary alcohol + NAD(+) = an aldehyde + H(+) + NADH;
CC Xref=Rhea:RHEA:10736, ChEBI:CHEBI:15378, ChEBI:CHEBI:15734,
CC ChEBI:CHEBI:17478, ChEBI:CHEBI:57540, ChEBI:CHEBI:57945; EC=1.1.1.1;
CC Evidence={ECO:0000250|UniProtKB:P0A9Q7};
CC -!- COFACTOR:
CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC Evidence={ECO:0000269|PubMed:32880589};
CC -!- SUBUNIT: Forms long filaments, called spirosomes.
CC {ECO:0000250|UniProtKB:P0A9Q7}.
CC -!- DOMAIN: Contains an N-terminal aldehyde dehydrogenase (ALDH) domain and
CC a C-terminal iron-dependent alcohol dehydrogenase (ADH) domain,
CC interconnected by a short linker. {ECO:0000250|UniProtKB:P0A9Q7}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene affects gene expression. It
CC leads to strong expression of non-functional flagella coupled to a
CC complete lack of the type 3 secretion system (T3SS), including the
CC structural proteins that comprise the secretory apparatus and its
CC effector proteins. Mutant displays a 'paralyzed' phenotype. It also
CC results in excretion of acetate into the surrounding environment, and
CC reduced binding to host cells, likely because it lacks the T3SS.
CC Deletion of the gene affects colonization and clinical disease in vivo.
CC {ECO:0000269|PubMed:24846743}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the aldehyde
CC dehydrogenase family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the iron-containing
CC alcohol dehydrogenase family. {ECO:0000305}.
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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_309768.1; NC_002695.1.
DR RefSeq; WP_000301651.1; NZ_SWKA01000005.1.
DR PDB; 6SCG; X-ray; 1.65 A; A/B=1-891.
DR PDB; 6SCI; X-ray; 1.95 A; A/B=1-891.
DR PDBsum; 6SCG; -.
DR PDBsum; 6SCI; -.
DR AlphaFoldDB; P0A9Q8; -.
DR SASBDB; P0A9Q8; -.
DR SMR; P0A9Q8; -.
DR STRING; 155864.EDL933_1943; -.
DR EnsemblBacteria; AAG56096; AAG56096; Z2016.
DR EnsemblBacteria; BAB35164; BAB35164; ECs_1741.
DR GeneID; 66674939; -.
DR GeneID; 913110; -.
DR KEGG; ece:Z2016; -.
DR KEGG; ecs:ECs_1741; -.
DR PATRIC; fig|386585.9.peg.1842; -.
DR eggNOG; COG1012; Bacteria.
DR eggNOG; COG1454; Bacteria.
DR HOGENOM; CLU_007207_2_2_6; -.
DR OMA; QWFKVPP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; Chromosome.
DR GO; GO:0008774; F:acetaldehyde dehydrogenase (acetylating) activity; IEA:UniProtKB-EC.
DR GO; GO:0004022; F:alcohol dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006066; P:alcohol metabolic process; IEA:InterPro.
DR GO; GO:0015976; P:carbon utilization; IEA:InterPro.
DR CDD; cd08178; AAD_C; 1.
DR Gene3D; 3.40.309.10; -; 1.
DR Gene3D; 3.40.605.10; -; 1.
DR InterPro; IPR034789; AAD_C.
DR InterPro; IPR001670; ADH_Fe/GldA.
DR InterPro; IPR018211; ADH_Fe_CS.
DR InterPro; IPR039697; Alcohol_dehydrogenase_Fe.
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 PANTHER; PTHR11496; PTHR11496; 1.
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 3D-structure; Iron; Metal-binding; Multifunctional enzyme; NAD;
KW Oxidoreductase; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT CHAIN 2..891
FT /note="Bifunctional aldehyde-alcohol dehydrogenase AdhE"
FT /id="PRO_0000087838"
FT REGION 2..440
FT /note="Aldehyde dehydrogenase"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT REGION 441..448
FT /note="Linker"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT REGION 449..891
FT /note="Alcohol dehydrogenase"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT ACT_SITE 246
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q9HTJ1"
FT BINDING 110..115
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 195
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 213
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 335
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 419
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 487
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG"
FT BINDING 519
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG"
FT BINDING 546..550
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG"
FT BINDING 597..598
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG"
FT BINDING 610
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 619
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P0A9Q7"
FT BINDING 638
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG"
FT BINDING 653
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG, ECO:0007744|PDB:6SCI"
FT BINDING 657
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG, ECO:0007744|PDB:6SCI"
FT BINDING 723
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG, ECO:0007744|PDB:6SCI"
FT BINDING 737
FT /ligand="Fe cation"
FT /ligand_id="ChEBI:CHEBI:24875"
FT /evidence="ECO:0000269|PubMed:32880589,
FT ECO:0007744|PDB:6SCG, ECO:0007744|PDB:6SCI"
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
