Aldehyde-alcohol dehydrogenase - Escherichia coli (strain K12)

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P0A9Q7 (ADHE_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 63. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Aldehyde-alcohol dehydrogenase

Including the following 3 domains:

Alcohol dehydrogenase
Short name=ADH
EC=1.1.1.1
Acetaldehyde dehydrogenase [acetylating]
Short name=ACDH
EC=1.2.1.10
Pyruvate-formate-lyase deactivase
Short name=PFL deactivase

Gene names

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

Organism

Escherichia coli (strain K12)

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 Reference proteome
Gene Ontology (GO)
Biological process	alcohol metabolic process Inferred from electronic annotation. Source: InterPro carbon utilization Inferred from electronic annotation. Source: InterPro
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: EcoliWiki alcohol dehydrogenase (NAD) activity Inferred from mutant phenotype. Source: EcoliWiki metal ion binding Inferred from electronic annotation. Source: InterPro
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

Removed Ref.1 Ref.2 Ref.7

Chain

2 – 891

890

Aldehyde-alcohol dehydrogenase

PRO_0000087837

Regions

Nucleotide binding

422 – 427

NAD Potential

Sites

Active site

246

By similarity

Amino acid modifications

Modified residue

358

N6-acetyllysine Ref.9

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9Q7 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 75469F57419C8C79
Show »

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

« Hide

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. 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. Strain: K12 / JW1106 and K12 / MG1655 / ATCC 47076.
+	Additional computationally mapped references.

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	NP_415757.1. NC_000913.2.
3D structure databases
ProteinModelPortal	P0A9Q7.
SMR	P0A9Q7. Positions 3-448, 451-862.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-35790N.
IntAct	P0A9Q7. 17 interactions.
MINT	MINT-1288364.
2D gel databases
ECO2DBASE	H097.3. 6TH EDITION.
Proteomic databases
PRIDE	P0A9Q7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	EBESCT00000002875; EBESCP00000002875; EBESCG00000002345. EBESCT00000002876; EBESCP00000002876; EBESCG00000002345. EBESCT00000015670; EBESCP00000014961; EBESCG00000014730.
GeneID	945837.
GenomeReviews	Gene locus JW1228 in contig AP009048_GR. Gene locus b1241 in contig U00096_GR.
KEGG	ecj:JW1228. eco:b1241.
PATRIC	32117740. VBIEscCol129921_1290.
Organism-specific databases
EchoBASE	EB0030.
EcoGene	EG10031. adhE.
Phylogenomic databases
eggNOG	COG1012.
GeneTree	EBGT00050000009177.
HOGENOM	HBG285847.
OMA	YVSVMAN.
PhylomeDB	P0A9Q7.
ProtClustDB	PRK13805.
Enzyme and pathway databases
BioCyc	EcoCyc:ADHE-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. IPR016163. Ald_DH_C. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH_dom. IPR012079. Bifunc_Ald/ADH. [Graphical view]
Gene3D	G3DSA:3.40.309.10. Aldehyde_dehydrogenase_C. 2 hits. G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
KO	K04072.
Pfam	PF00171. Aldedh. 1 hit. PF00465. Fe-ADH. 1 hit. [Graphical view]
PIRSF	PIRSF000111. ALDH_ADH. 1 hit.
SUPFAM	SSF53720. Aldehyde_DH/Histidinol_DH. 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:	January 25, 2012
This is version 63 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Including the following 3 domains:

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

2D gel databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Entry information

Relevant documents