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P0A9Q8 (ADHE_ECO57) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 62. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Aldehyde-alcohol dehydrogenase

Including the following 3 domains:

  1. Alcohol dehydrogenase
    Short name=ADH
    EC=1.1.1.1
  2. Acetaldehyde dehydrogenase [acetylating]
    Short name=ACDH
    EC=1.2.1.10
  3. Pyruvate-formate-lyase deactivase
    Short name=PFL deactivase
Gene names
Name:adhE
Ordered Locus Names:Z2016, ECs1741
OrganismEscherichia coli O157:H7 [Complete proteome] [HAMAP]
Taxonomic identifier83334 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length891 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 891890Aldehyde-alcohol dehydrogenase
PRO_0000087838

Regions

Nucleotide binding422 – 4276NAD Potential

Sites

Active site2461 By similarity

Amino acid modifications

Modified residue3581N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P0A9Q8 [UniParc].

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

FASTA89196,127
        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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE005174 Genomic DNA. Translation: AAG56096.1.
BA000007 Genomic DNA. Translation: BAB35164.1.
PIRE90846.
RefSeqNP_287484.1. NC_002655.2.
NP_309768.1. NC_002695.1.

3D structure databases

ProteinModelPortalP0A9Q8.
SMRP0A9Q8. Positions 3-448, 450-864.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

MINTMINT-1288351.
STRING155864.Z2016.

Proteomic databases

PRIDEP0A9Q8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAG56096; AAG56096; Z2016.
BAB35164; BAB35164; BAB35164.
GeneID913110.
960491.
KEGGece:Z2016.
ecs:ECs1741.
PATRIC18352746. VBIEscCol44059_1596.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000025256.
KOK04072.
OMAWHKLPSS.
OrthoDBEOG6TFCQS.
ProtClustDBPRK13805.

Enzyme and pathway databases

BioCycECOL386585:GJFA-1725-MONOMER.
ECOO157:ADHE-MONOMER.

Family and domain databases

Gene3D3.40.309.10. 2 hits.
3.40.605.10. 1 hit.
InterProIPR001670. 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]
PfamPF00171. Aldedh. 1 hit.
PF00465. Fe-ADH. 1 hit.
[Graphical view]
PIRSFPIRSF000111. ALDH_ADH. 1 hit.
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameADHE_ECO57
AccessionPrimary (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: March 19, 2014
This is version 62 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families