Aldehyde-alcohol dehydrogenase - Escherichia coli O157:H7

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P0A9Q8 (ADHE_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. History...

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

Documents (1) |

Third-party data

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Names·Attributes·General annotation·Ontologies·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
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
Molecular_function	acetaldehyde dehydrogenase (acetylating) activity Inferred from electronic annotation. Source: EC alcohol dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC metal ion binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 891

890

Aldehyde-alcohol dehydrogenase

PRO_0000087838

Regions

Nucleotide binding

422 – 427

NAD Potential

Sites

Active site

246

By similarity

Amino acid modifications

Modified residue

358

N6-acetyllysine By similarity

Sequences

Sequence

Length

Mass (Da)

Tools

P0A9Q8 [UniParc].

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

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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. Blattner F.R. Nature 409:529-533(2001) [PubMed] [Europe PMC] [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] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: O157:H7 / Sakai / RIMD 0509952 / EHEC.
+	Additional computationally mapped references.

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. NC_002655.2. NP_309768.1. NC_002695.1.
3D structure databases
ProteinModelPortal	P0A9Q8.
SMR	P0A9Q8. Positions 3-448, 465-862.
ModBase	Search...
Protein-protein interaction databases
MINT	MINT-1288351.
STRING	155864.Z2016.
Proteomic databases
PRIDE	P0A9Q8.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	AAG56096; AAG56096; Z2016. BAB35164; BAB35164; BAB35164.
GeneID	913110. 960491.
KEGG	ece:Z2016. ecs:ECs1741.
PATRIC	18352746. VBIEscCol44059_1596.
Organism-specific databases
CMR	Search...
Phylogenomic databases
eggNOG	COG1012.
HOGENOM	HOG000025256.
KO	K04072.
OMA	YVSVMAN.
ProtClustDB	PRK13805.
Enzyme and pathway databases
BioCyc	ECOL386585:GJFA-1725-MONOMER.
Family and domain databases
Gene3D	3.40.309.10. 2 hits. 3.40.605.10. 1 hit.
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]
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_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:	May 1, 2013
This is version 58 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

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·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

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Family and domain databases

Entry information

Relevant documents