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Protein

Acetaldehyde dehydrogenase

Gene

mhpF

Organism
Escherichia coli O9:H4 (strain HS)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the conversion of acetaldehyde to acetyl-CoA, using NAD+ and coenzyme A. Is the final enzyme in the meta-cleavage pathway for the degradation of aromatic compounds.UniRule annotation

Catalytic activityi

Acetaldehyde + CoA + NAD+ = acetyl-CoA + NADH.UniRule annotation

Pathway: 3-phenylpropanoate degradation

This protein is involved in the pathway 3-phenylpropanoate degradation, which is part of Aromatic compound metabolism.UniRule annotation
View all proteins of this organism that are known to be involved in the pathway 3-phenylpropanoate degradation and in Aromatic compound metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei131 – 1311Acyl-thioester intermediateUniRule annotation
Binding sitei289 – 2891NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi11 – 144NADUniRule annotation
Nucleotide bindingi162 – 1709NADUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciECOL331112:GHHI-413-MONOMER.
UniPathwayiUPA00714.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenaseUniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating]UniRule annotation
Gene namesi
Name:mhpFUniRule annotation
Ordered Locus Names:EcHS_A0415
OrganismiEscherichia coli O9:H4 (strain HS)
Taxonomic identifieri331112 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 316316Acetaldehyde dehydrogenasePRO_0000337981Add
BLAST

Interactioni

Subunit structurei

Interacts with MhpE.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA7ZWZ8.
SMRiA7ZWZ8. Positions 3-308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OMAiHQGNVNM.
OrthoDBiEOG6H1PXH.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.

Sequencei

Sequence statusi: Complete.

A7ZWZ8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSKRKVAIIG SGNIGTDLMI KILRHGQHLE MAVMVGIDPQ SDGLARARRM
60 70 80 90 100
GVATTHEGVI GLMNMPEFAD IDIVFDATSA GAHVKNDAAL REAKPDIRLI
110 120 130 140 150
DLTPAAIGPY CVPVVNLEAN VDQLNVNMVT CGGQATIPMV AAVSRVARVH
160 170 180 190 200
YAEIIASIAS KSAGPGTRAN IDEFTETTSR AIEVVGGAAK GKAIIVLNPA
210 220 230 240 250
EPPLMMRDTV YVLSDEASQD DIEASINEMA EAVQAYVPGY RLKQRVQFEV
260 270 280 290 300
IPQDKPVNLP GVGQFSGLKT AVWLEVEGAA HYLPAYAGNL DIMTSSALAT
310
AEKMAQSLAR KAGEAA
Length:316
Mass (Da):33,442
Last modified:October 23, 2007 - v1
Checksum:iA6918BDA5EF4876B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV04802.1.
RefSeqiWP_000044314.1. NC_009800.1.

Genome annotation databases

EnsemblBacteriaiABV04802; ABV04802; EcHS_A0415.
KEGGiecx:EcHS_A0415.
PATRICi18310828. VBIEscCol77814_0408.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000802 Genomic DNA. Translation: ABV04802.1.
RefSeqiWP_000044314.1. NC_009800.1.

3D structure databases

ProteinModelPortaliA7ZWZ8.
SMRiA7ZWZ8. Positions 3-308.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV04802; ABV04802; EcHS_A0415.
KEGGiecx:EcHS_A0415.
PATRICi18310828. VBIEscCol77814_0408.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK04073.
OMAiHQGNVNM.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

UniPathwayiUPA00714.
BioCyciECOL331112:GHHI-413-MONOMER.

Family and domain databases

Gene3Di3.40.50.720. 1 hit.
HAMAPiMF_01657. Ac_ald_DH_ac.
InterProiIPR003361. Acetaldehyde_dehydrogenase.
IPR015426. Acetylaldehyde_DH_C.
IPR016040. NAD(P)-bd_dom.
IPR000534. Semialdehyde_DH_NAD-bd.
[Graphical view]
PfamiPF09290. AcetDehyd-dimer. 1 hit.
PF01118. Semialdhyde_dh. 1 hit.
[Graphical view]
PIRSFiPIRSF015689. Actaldh_dh_actl. 1 hit.
SMARTiSM00859. Semialdhyde_dh. 1 hit.
[Graphical view]
TIGRFAMsiTIGR03215. ac_ald_DH_ac. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The pangenome structure of Escherichia coli: comparative genomic analysis of E. coli commensal and pathogenic isolates."
    Rasko D.A., Rosovitz M.J., Myers G.S.A., Mongodin E.F., Fricke W.F., Gajer P., Crabtree J., Sebaihia M., Thomson N.R., Chaudhuri R., Henderson I.R., Sperandio V., Ravel J.
    J. Bacteriol. 190:6881-6893(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: HS.

Entry informationi

Entry nameiACDH_ECOHS
AccessioniPrimary (citable) accession number: A7ZWZ8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 10, 2008
Last sequence update: October 23, 2007
Last modified: June 24, 2015
This is version 56 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.