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Protein

Acetaldehyde dehydrogenase 1

Gene

Mpe_A2267

Organism
Methylibium petroleiphilum (strain PM1)
Status
Reviewed-Annotation score: Annotation score: 2 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

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei130 – 1301Acyl-thioester intermediateUniRule annotation
Binding sitei272 – 2721NADUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi161 – 1699NADUniRule annotation

GO - Molecular functioni

  1. acetaldehyde dehydrogenase (acetylating) activity Source: UniProtKB-HAMAP
  2. NAD binding Source: UniProtKB-HAMAP

GO - Biological processi

  1. aromatic compound catabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Biological processi

Aromatic hydrocarbons catabolism

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMPET420662:GHBE-2297-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Acetaldehyde dehydrogenase 1UniRule annotation (EC:1.2.1.10UniRule annotation)
Alternative name(s):
Acetaldehyde dehydrogenase [acetylating] 1UniRule annotation
Gene namesi
Ordered Locus Names:Mpe_A2267
OrganismiMethylibium petroleiphilum (strain PM1)
Taxonomic identifieri420662 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaBetaproteobacteriaBurkholderialesMethylibium
ProteomesiUP000000366: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 303303Acetaldehyde dehydrogenase 1PRO_0000387666Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi420662.Mpe_A2267.

Structurei

3D structure databases

ProteinModelPortaliA2SI34.
SMRiA2SI34. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the acetaldehyde dehydrogenase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
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.

A2SI34-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKKIKCALIG PGNIGTDLLA KLQRSPVLEP VWMVGIDPGS DGLKRARDAG
60 70 80 90 100
LKTTAEGVDG LLPHVKADGV QIAFDATSAY VHAENSRKLN ALGVMMIDLT
110 120 130 140 150
PAAIGPFCVP PVNLKQHLGR REMNVNMVTC GGQATIPMVA AVSQVQAVAY
160 170 180 190 200
GEIVATVSSR SVGPGTRKNI DEFTRTTAGA VEKVGGAKKG KAIIIINPAE
210 220 230 240 250
PPLIMRDTVH CLTVDEPDRD RITASIHQMI REVQKYVPGY KLVNGPVFDG
260 270 280 290 300
KRVSVFMEVE GLGDYLPKYA GNLDIMTAAA ARTAEMFAEE LIAGTLKLEA

VPA
Length:303
Mass (Da):32,208
Last modified:March 6, 2007 - v1
Checksum:i6EA1E1CB3AABB060
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM95223.1.
RefSeqiYP_001021458.1. NC_008825.1.

Genome annotation databases

EnsemblBacteriaiABM95223; ABM95223; Mpe_A2267.
GeneIDi4785106.
KEGGimpt:Mpe_A2267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000555 Genomic DNA. Translation: ABM95223.1.
RefSeqiYP_001021458.1. NC_008825.1.

3D structure databases

ProteinModelPortaliA2SI34.
SMRiA2SI34. Positions 2-293.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi420662.Mpe_A2267.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM95223; ABM95223; Mpe_A2267.
GeneIDi4785106.
KEGGimpt:Mpe_A2267.

Phylogenomic databases

eggNOGiCOG4569.
HOGENOMiHOG000052149.
KOiK18366.
OMAiHQGNVNM.
OrthoDBiEOG6H1PXH.

Enzyme and pathway databases

BioCyciMPET420662:GHBE-2297-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. "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-proteobacterium Methylibium petroleiphilum PM1."
    Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., Hristova K.R.
    J. Bacteriol. 189:1931-1945(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: PM1.

Entry informationi

Entry nameiACDH1_METPP
AccessioniPrimary (citable) accession number: A2SI34
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 3, 2009
Last sequence update: March 6, 2007
Last modified: January 7, 2015
This is version 57 of the entry and version 1 of the sequence. [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

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.