Reviewed, UniProtKB/Swiss-Prot P0A9Q8 (ADHE_ECO57)

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
Ordered Locus Names:	Z2016, ECs1741

Organism

Escherichia coli O157:H7 [Complete proteome] [HAMAP]

Taxonomic identifier

83334 [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	Inferred from homology.

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 By similarity.
Catalytic activity	An alcohol + NAD+ = an aldehyde or ketone + NADH. Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.
Cofactor	Iron By similarity.
Subunit structure	Seems to form a rod shaped polymer composed of about 40 identical subunits By similarity.
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 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
Molecular function	acetaldehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 891	890	Aldehyde-alcohol dehydrogenase		PRO_0000087838
Regions
	Nucleotide binding	422 – 427	6	NAD Potential
Sites
	Active site	246	1	By similarity
Amino acid modifications
	Modified residue	358	1	N6-acetyllysine By similarity

Sequences

	Sequence		Length	Mass (Da)
	P0A9Q8-1 [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

[1]

"Genome sequence of enterohaemorrhagic Escherichia coli O157:H7." Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J., Davis N.W. , Lim A., Dimalanta E.T., Potamousis K., Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A., Blattner F.R. Nature 409:529-533(2001) [PubMed: 11206551] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / EDL933 / ATCC 700927 / EHEC.

[2]

"Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and genomic comparison with a laboratory strain K-12." Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K., Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T. , Kuhara S., Shiba T., Hattori M., Shinagawa H. DNA Res. 8:11-22(2001) [PubMed: 11258796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AE005174 Genomic DNA. Translation: AAG56096.1. BA000007 Genomic DNA. Translation: BAB35164.1.
PIR	E90846.
RefSeq	NP_287484.1. NP_309768.1.
3D structure databases
ModBase	Search...
Proteomic databases
PRIDE	P0A9Q8.
Genome annotation databases
GeneID	913110. 960491.
GenomeReviews	Gene locus Z2016 in contig AE005174_GR. Gene locus ECs1741 in contig BA000007_GR.
KEGG	ece:Z2016. ecs:ECs1741.
Organism-specific databases
CMR	Search...
Phylogenomic databases
HOGENOM	HBG285847.
Enzyme and pathway databases
BioCyc	ECOL83334:ECS1741-MONOMER.
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_ECO57

Accession

Primary (citable) accession number: P0A9Q8
Secondary accession number(s): P17547

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	January 23, 2007
Last modified:	January 19, 2010
This is version 32 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)