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P0A9Q8

- ADHE_ECO57

UniProt

P0A9Q8 - ADHE_ECO57

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Protein

Aldehyde-alcohol dehydrogenase

Gene

adhE

Organism
Escherichia coli O157:H7
Status
Reviewed - Annotation score: 3 out of 5- 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

An alcohol + NAD+ = an aldehyde or ketone + NADH.
Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.

Cofactori

Iron.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei246 – 2461By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi422 – 4276NADSequence Analysis

GO - Molecular functioni

  1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-EC
  2. alcohol dehydrogenase (NAD) activity Source: UniProtKB-EC
  3. metal ion binding Source: InterPro

GO - Biological processi

  1. alcohol metabolic process Source: InterPro
  2. carbon utilization Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

Iron, NAD

Enzyme and pathway databases

BioCyciECOL386585:GJFA-1725-MONOMER.
ECOO157:ADHE-MONOMER.

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 lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000000558: Chromosome, UP000002519: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 891890Aldehyde-alcohol dehydrogenasePRO_0000087838Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei358 – 3581N6-acetyllysineBy similarity

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

MINTiMINT-1288351.
STRINGi155864.Z2016.

Structurei

3D structure databases

ProteinModelPortaliP0A9Q8.
SMRiP0A9Q8. Positions 3-448, 450-864.
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

eggNOGiCOG1012.
HOGENOMiHOG000025256.
KOiK04072.
OMAiSPLLAMY.
OrthoDBiEOG6TFCQS.

Family and domain databases

Gene3Di3.40.309.10. 2 hits.
3.40.605.10. 1 hit.
InterProiIPR001670. 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]
PfamiPF00171. Aldedh. 1 hit.
PF00465. Fe-ADH. 1 hit.
[Graphical view]
PIRSFiPIRSF000111. ALDH_ADH. 1 hit.
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view]

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:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56096.1.
BA000007 Genomic DNA. Translation: BAB35164.1.
PIRiE90846.
RefSeqiNP_287484.1. NC_002655.2.
NP_309768.1. NC_002695.1.

Genome annotation databases

EnsemblBacteriaiAAG56096; AAG56096; Z2016.
BAB35164; BAB35164; BAB35164.
GeneIDi913110.
960491.
KEGGiece:Z2016.
ecs:ECs1741.
PATRICi18352746. VBIEscCol44059_1596.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AE005174 Genomic DNA. Translation: AAG56096.1 .
BA000007 Genomic DNA. Translation: BAB35164.1 .
PIRi E90846.
RefSeqi NP_287484.1. NC_002655.2.
NP_309768.1. NC_002695.1.

3D structure databases

ProteinModelPortali P0A9Q8.
SMRi P0A9Q8. Positions 3-448, 450-864.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

MINTi MINT-1288351.
STRINGi 155864.Z2016.

Proteomic databases

PRIDEi P0A9Q8.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAG56096 ; AAG56096 ; Z2016 .
BAB35164 ; BAB35164 ; BAB35164 .
GeneIDi 913110.
960491.
KEGGi ece:Z2016.
ecs:ECs1741.
PATRICi 18352746. VBIEscCol44059_1596.

Phylogenomic databases

eggNOGi COG1012.
HOGENOMi HOG000025256.
KOi K04072.
OMAi SPLLAMY.
OrthoDBi EOG6TFCQS.

Enzyme and pathway databases

BioCyci ECOL386585:GJFA-1725-MONOMER.
ECOO157:ADHE-MONOMER.

Family and domain databases

Gene3Di 3.40.309.10. 2 hits.
3.40.605.10. 1 hit.
InterProi 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 ]
Pfami PF00171. Aldedh. 1 hit.
PF00465. Fe-ADH. 1 hit.
[Graphical view ]
PIRSFi PIRSF000111. ALDH_ADH. 1 hit.
SUPFAMi SSF53720. SSF53720. 1 hit.
PROSITEi PS00913. ADH_IRON_1. 1 hit.
PS00060. ADH_IRON_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. 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.

Entry informationi

Entry nameiADHE_ECO57
AccessioniPrimary (citable) accession number: P0A9Q8
Secondary accession number(s): P17547
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 23, 2007
Last modified: October 1, 2014
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3