Reviewed, UniProtKB/Swiss-Prot P0A9Q7 (ADHE_ECOLI)

Names and origin

Protein names

Recommended name:
    Aldehyde-alcohol dehydrogenase
Including the following 3 domains:
    1- Recommended name:
            Alcohol dehydrogenase
                Short name=ADH
              EC=1.1.1.1
    2- Recommended name:
            Acetaldehyde dehydrogenase [acetylating]
                Short name=ACDH
              EC=1.2.1.10
    3- Recommended name:
            Pyruvate-formate-lyase deactivase
                Short name=PFL deactivase

Gene names

Name:	adhE
Synonyms:	ana
Ordered Locus Names:	b1241, JW1228

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	891 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	This enzyme has three activities: ADH, ACDH, and PFL-deactivase. In aerobic conditions it acts as a hydrogen peroxide scavenger. The PFL deactivase activity catalyzes the quenching of the pyruvate-formate-lyase catalyst in an iron, NAD, and CoA dependent reaction.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH. Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.
Cofactor	Iron.
Subunit structure	Seems to form a rod shaped polymer composed of about 40 identical subunits.
Induction	Under anaerobic conditions in the absence of nitrate.
Sequence similarities	In the N-terminal section; belongs to the aldehyde dehydrogenase family. In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.

Ontologies

Keywords
Ligand	Iron NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Complete proteome Direct protein sequencing Multifunctional enzyme
Gene Ontology (GO)
Biological process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro carbon utilization Inferred from electronic annotation. Source: InterPro oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB membrane Inferred from direct assay. Source: UniProtKB
Molecular function	acetaldehyde dehydrogenase (acetylating) activity Inferred from mutant phenotype. Source: UniProtKB alcohol dehydrogenase (NAD) activity Inferred from mutant phenotype. Source: UniProtKB iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
rpsB	P0A7V0	1	EBI-543417,EBI-543439

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.1 Ref.2 Ref.7
	Chain	2 – 891	890	Aldehyde-alcohol dehydrogenase		PRO_0000087837
Regions
	Nucleotide binding	422 – 427	6	NAD Potential
Sites
	Active site	246	1	By similarity
Amino acid modifications
	Modified residue	358	1	N6-acetyllysine Ref.9

Sequences

	Sequence		Length	Mass (Da)
	P0A9Q7-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 75469F57419C8C79	FASTA	891	96,127
	10 20 30 40 50 60 MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA KMAVAESGMG 70 80 90 100 110 120 IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI AEPIGIICGI VPTTNPTSTA 130 140 150 160 170 180 IFKSLISLKT RNAIIFSPHP RAKDATNKAA DIVLQAAIAA GAPKDLIGWI DQPSVELSNA 190 200 210 220 230 240 LMHHPDINLI LATGGPGMVK AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF 250 260 270 280 290 300 DNGVICASEQ SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP 310 320 330 340 350 360 AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE DAVEKAEKLV 370 380 390 400 410 420 AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA SQGGIGDLYN FKLAPSLTLG 430 440 450 460 470 480 CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN MLWHKLPKSI YFRRGSLPIA LDEVITDGHK 490 500 510 520 530 540 RALIVTDRFL FNNGYADQIT SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI 550 560 570 580 590 600 IALGGGSPMD AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG 610 620 630 640 650 660 TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG GLDAVTHAME 670 680 690 700 710 720 AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR ERVHSAATIA GIAFANAFLG 730 740 750 760 770 780 VCHSMAHKLG SQFHIPHGLA NALLICNVIR YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD 790 800 810 820 830 840 HLGLSAPGDR TAAKIEKLLA WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ 850 860 870 880 890 CTGANPRYPL ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and sequence analysis of the fermentative alcohol-dehydrogenase-encoding gene of Escherichia coli." Goodlove P.E., Cunningham P.R., Parker J., Clark D.P. Gene 85:209-214(1989) [PubMed: 2695398] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-11.
[2]	"Pyruvate-formate-lyase-deactivase and acetyl-CoA reductase activities of Escherichia coli reside on a polymeric protein particle encoded by adhE." Kessler D., Leibrecht I., Knappe J. FEBS Lett. 281:59-63(1991) [PubMed: 2015910] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-7, CHARACTERIZATION. Strain: K12.
[3]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. , Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]	"Filling the gap between hns and adhE in Escherichia coli K12." Danchin A., Krin E. Microbiology 141:959-960(1995) [PubMed: 7773397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 849-891. Strain: K12.
[7]	"Monoclonal antibodies to spirosin of Yersinia enterocolitica and analysis of the localization of spirosome by use of them." Yamato M., Takahashi Y., Tomotake H., Ota F., Hirota K., Yamaguchi K. Microbiol. Immunol. 38:177-182(1994) [PubMed: 7521508] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-21.
[8]	"Novel antioxidant role of alcohol dehydrogenase E from Escherichia coli." Echave P., Tamarit J., Cabiscol E., Ros J. J. Biol. Chem. 278:30193-30198(2003) [PubMed: 12783863] [Abstract] Cited for: ANTIOXIDANT ROLE OF ADHE. Strain: K12 / MC4100 / ATCC 35695 / DSM 6574.
[9]	"Lysine acetylation is a highly abundant and evolutionarily conserved modification in Escherichia coli." Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., Grishin N.V., Zhao Y. Mol. Cell. Proteomics 8:215-225(2009) [PubMed: 18723842] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-358, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	X59263 Genomic DNA. Translation: CAA41955.1. M33504 Genomic DNA. Translation: AAA23420.1. U00096 Genomic DNA. Translation: AAC74323.1. AP009048 Genomic DNA. Translation: BAA36121.1. X67326 Genomic DNA. Translation: CAA47743.1.
PIR	DEEC. JS0406.
RefSeq	AP_001865.1. NP_415757.1.
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	P0A9Q7. 15 interactions.
STRING	P0A9Q7.
2-D gel databases
ECO2DBASE	H097.3. 6TH EDITION.
Proteomic databases
PRIDE	P0A9Q7.
Genome annotation databases
GeneID	945837.
GenomeReviews	Gene locus JW1228 in contig AP009048_GR. Gene locus b1241 in contig U00096_GR.
KEGG	ecj:JW1228. eco:b1241.
Organism-specific databases
EchoBASE	EB0030.
EcoGene	EG10031. adhE.
CMR	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HBG285847.
OMA	AFAHEKL.
Enzyme and pathway databases
BioCyc	EcoCyc:ADHE-MONOMER. ECOL168927:B1241-MONOMER. MetaCyc:ADHE-MONOMER.
Gene expression databases
Genevestigator	P0A9Q7.
Family and domain databases
InterPro	IPR001670. ADH_Fe. IPR018211. ADH_Fe_CS. IPR016161. Ald_DH/histidinol_DH. IPR015590. Aldehyde_DH. IPR012079. Bifunc_Ald/AlcDH. [Graphical view]
Pfam	PF00171. Aldedh. 1 hit. PF00465. Fe-ADH. 1 hit. [Graphical view]
PIRSF	PIRSF000111. ALDH_ADH. 1 hit.
PROSITE	PS00913. ADH_IRON_1. 1 hit. PS00060. ADH_IRON_2. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

ADHE_ECOLI

Accession

Primary (citable) accession number: P0A9Q7
Secondary accession number(s): P17547

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 45 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)