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Protein

Aldehyde-alcohol dehydrogenase

Gene

adhE

Organism
Escherichia coli O157:H7
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).By similarity

Catalytic activityi

A primary alcohol + NAD+ = an aldehyde + NADH.
A secondary alcohol + NAD+ = a ketone + NADH.
Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.

Cofactori

Fe cationBy similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei246By similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi422 – 427NADSequence analysis6

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionMultifunctional enzyme, Oxidoreductase
LigandIron, NAD

Names & Taxonomyi

Protein namesi
Recommended name:
Aldehyde-alcohol dehydrogenase
Including the following 3 domains:
Alcohol dehydrogenase (EC:1.1.1.1)
Short name:
ADH
Acetaldehyde dehydrogenase [acetylating] (EC:1.2.1.10)
Short name:
ACDH
Pyruvate-formate-lyase deactivase
Short name:
PFL deactivase
Gene namesi
Name:adhE
Ordered Locus Names:Z2016, ECs1741
OrganismiEscherichia coli O157:H7
Taxonomic identifieri83334 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000558 Componenti: Chromosome
  • UP000002519 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000878382 – 891Aldehyde-alcohol dehydrogenaseAdd BLAST890

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei358N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

PRIDEiP0A9Q8

Interactioni

Subunit structurei

Seems to form a rod shaped polymer composed of about 40 identical subunits.By similarity

Protein-protein interaction databases

STRINGi155864.Z2016

Structurei

3D structure databases

ProteinModelPortaliP0A9Q8
SMRiP0A9Q8
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

In the N-terminal section; belongs to the aldehyde dehydrogenase family.Curated
In the C-terminal section; belongs to the iron-containing alcohol dehydrogenase family.Curated

Phylogenomic databases

eggNOGiENOG4108EKI Bacteria
COG1012 LUCA
COG1454 LUCA
HOGENOMiHOG000025256
KOiK04072
OMAiWHKLPSS

Family and domain databases

CDDicd08178 AAD_C, 1 hit
Gene3Di3.40.309.10, 1 hit
3.40.605.10, 2 hits
InterProiView protein in InterPro
IPR034789 AAD_C
IPR001670 ADH_Fe/GldA
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
PfamiView protein in Pfam
PF00171 Aldedh, 1 hit
PF00465 Fe-ADH, 1 hit
PIRSFiPIRSF000111 ALDH_ADH, 1 hit
SUPFAMiSSF53720 SSF53720, 1 hit
PROSITEiView protein in PROSITE
PS00913 ADH_IRON_1, 1 hit
PS00060 ADH_IRON_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A9Q8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAVTNVAELN ALVERVKKAQ REYASFTQEQ VDKIFRAAAL AAADARIPLA
60 70 80 90 100
KMAVAESGMG IVEDKVIKNH FASEYIYNAY KDEKTCGVLS EDDTFGTITI
110 120 130 140 150
AEPIGIICGI VPTTNPTSTA IFKSLISLKT RNAIIFSPHP RAKDATNKAA
160 170 180 190 200
DIVLQAAIAA GAPKDLIGWI DQPSVELSNA LMHHPDINLI LATGGPGMVK
210 220 230 240 250
AAYSSGKPAI GVGAGNTPVV IDETADIKRA VASVLMSKTF DNGVICASEQ
260 270 280 290 300
SVVVVDSVYD AVRERFATHG GYLLQGKELK AVQDVILKNG ALNAAIVGQP
310 320 330 340 350
AYKIAELAGF SVPENTKILI GEVTVVDESE PFAHEKLSPT LAMYRAKDFE
360 370 380 390 400
DAVEKAEKLV AMGGIGHTSC LYTDQDNQPA RVSYFGQKMK TARILINTPA
410 420 430 440 450
SQGGIGDLYN FKLAPSLTLG CGSWGGNSIS ENVGPKHLIN KKTVAKRAEN
460 470 480 490 500
MLWHKLPKSI YFRRGSLPIA LDEVITDGHK RALIVTDRFL FNNGYADQIT
510 520 530 540 550
SVLKAAGVET EVFFEVEADP TLSIVRKGAE LANSFKPDVI IALGGGSPMD
560 570 580 590 600
AAKIMWVMYE HPETHFEELA LRFMDIRKRI YKFPKMGVKA KMIAVTTTSG
610 620 630 640 650
TGSEVTPFAV VTDDATGQKY PLADYALTPD MAIVDANLVM DMPKSLCAFG
660 670 680 690 700
GLDAVTHAME AYVSVLASEF SDGQALQALK LLKEYLPASY HEGSKNPVAR
710 720 730 740 750
ERVHSAATIA GIAFANAFLG VCHSMAHKLG SQFHIPHGLA NALLICNVIR
760 770 780 790 800
YNANDNPTKQ TAFSQYDRPQ ARRRYAEIAD HLGLSAPGDR TAAKIEKLLA
810 820 830 840 850
WLETLKAELG IPKSIREAGV QEADFLANVD KLSEDAFDDQ CTGANPRYPL
860 870 880 890
ISELKQILLD TYYGRDYVEG ETAAKKEAAP AKAEKKAKKS A
Length:891
Mass (Da):96,127
Last modified:January 23, 2007 - v2
Checksum:i75469F57419C8C79
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005174 Genomic DNA Translation: AAG56096.1
BA000007 Genomic DNA Translation: BAB35164.1
PIRiE90846
RefSeqiNP_309768.1, NC_002695.1
WP_000301651.1, NZ_NOKN01000002.1

Genome annotation databases

EnsemblBacteriaiAAG56096; AAG56096; Z2016
BAB35164; BAB35164; BAB35164
GeneIDi913110
KEGGiece:Z2016
ecs:ECs1741
PATRICifig|386585.9.peg.1842

Similar proteinsi

Entry informationi

Entry nameiADHE_ECO57
AccessioniPrimary (citable) accession number: P0A9Q8
Secondary accession number(s): P17547
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: June 20, 2018
This is version 88 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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