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P20000 (ALDH2_BOVIN) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 111. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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 dehydrogenase, mitochondrial

EC=1.2.1.3
Alternative name(s):
ALDH class 2
ALDH-E2
ALDHI
Gene names
Name:ALDH2
OrganismBos taurus (Bovine) [Reference proteome]
Taxonomic identifier9913 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraBovidaeBovinaeBos

Protein attributes

Sequence length520 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathway

Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.

Subunit structure

Homotetramer.

Subcellular location

Mitochondrion matrix.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrial matrix

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaldehyde dehydrogenase (NAD) activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2121Mitochondrion Ref.4
Chain22 – 520499Aldehyde dehydrogenase, mitochondrial
PRO_0000007167

Regions

Nucleotide binding265 – 2706NAD By similarity

Sites

Active site2881Proton acceptor
Active site3221Nucleophile
Site1891Transition state stabilizer

Amino acid modifications

Modified residue551N6-acetyllysine By similarity
Modified residue761N6-acetyllysine By similarity
Modified residue1621N6-acetyllysine By similarity
Modified residue3711N6-acetyllysine By similarity
Modified residue3781N6-acetyllysine By similarity
Modified residue3861N6-acetyllysine By similarity
Modified residue4291N6-acetyllysine By similarity
Modified residue4311N6-acetyllysine By similarity
Modified residue4441N6-acetyllysine By similarity
Modified residue4541N6-acetyllysine By similarity

Experimental info

Sequence conflict2891L → I no nucleotide entry Ref.1
Sequence conflict2891L → I no nucleotide entry Ref.3
Sequence conflict3851A → L no nucleotide entry Ref.1
Sequence conflict3851A → L no nucleotide entry Ref.3
Sequence conflict4091V → L no nucleotide entry Ref.1
Sequence conflict4091V → L no nucleotide entry Ref.3

Secondary structure

.................................................................................. 520
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P20000 [UniParc].

Last modified July 1, 2008. Version 2.
Checksum: 713FC1EE8F82B2C4

FASTA52056,653
        10         20         30         40         50         60 
MLRAVALAAA RLGPRQGRRL LSAATQAVPT PNQQPEVLYN QIFINNEWHD AVSKKTFPTV 

        70         80         90        100        110        120 
NPSTGDVICH VAEGDKADVD RAVKAARAAF QLGSPWRRMD ASERGRLLNR LADLIERDRT 

       130        140        150        160        170        180 
YLAALETLDN GKPYIISYLV DLDMVLKCLR YYAGWADKYH GKTIPIDGDY FSYTRHEPVG 

       190        200        210        220        230        240 
VCGQIIPWNF PLLMQAWKLG PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNV 

       250        260        270        280        290        300 
IPGFGPTAGA AIASHEDVDK VAFTGSTEVG HLIQVAAGKS NLKRVTLELG GKSPNIIMSD 

       310        320        330        340        350        360 
ADMDWAVEQA HFALFFNQGQ CCCAGSRTFV QEDIYAEFVE RSVARAKSRV VGNPFDSRTE 

       370        380        390        400        410        420 
QGPQVDETQF KKVLGYIKSG KEEGAKLLCG GGAAADRGYF IQPTVFGDVQ DGMTIAKEEI 

       430        440        450        460        470        480 
FGPVMQILKF KSMEEVVGRA NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWVNCYDVFG 

       490        500        510        520 
AQSPFGGYKL SGSGRELGEY GLQAYTEVKT VTVRVPQKNS 

« Hide

References

« Hide 'large scale' references
[1]"Sequence of the precursor of bovine liver mitochondrial aldehyde dehydrogenase as determined from its cDNA, its gene, and its functionality."
Guan K., Weiner H.
Arch. Biochem. Biophys. 277:351-360(1990) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]NIH - Mammalian Gene Collection (MGC) project
Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: Hereford.
Tissue: Ascending colon.
[3]"Primary structures of rat and bovine liver mitochondrial aldehyde dehydrogenases deduced from cDNA sequences."
Farres J., Guan K.-L., Weiner H.
Eur. J. Biochem. 180:67-74(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 92-520.
[4]"Purification and characterization of bovine brain gamma-aminobutyraldehyde dehydrogenase."
Lee J.E., Cho Y.D.
Biochem. Biophys. Res. Commun. 189:450-454(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 22-34.
Tissue: Brain.
[5]"Structure of mitochondrial aldehyde dehydrogenase: the genetic component of ethanol aversion."
Steinmetz C.G., Xie P., Weiner H., Hurley T.D.
Structure 5:701-711(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS).

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BC116084 mRNA. Translation: AAI16085.1.
PIRS09030.
RefSeqNP_001068835.1. NM_001075367.1.
UniGeneBt.44041.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1A4ZX-ray2.75A/B/C/D22-520[»]
1AG8X-ray2.65A/B/C/D22-520[»]
ProteinModelPortalP20000.
SMRP20000. Positions 28-520.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9913.ENSBTAP00000011521.

Proteomic databases

PaxDbP20000.
PRIDEP20000.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSBTAT00000011521; ENSBTAP00000011521; ENSBTAG00000008743.
GeneID508629.
KEGGbta:508629.

Organism-specific databases

CTD217.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00550000074289.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP20000.
KOK00128.
OMAVAYHIYE.
OrthoDBEOG7PS1F7.
TreeFamTF300455.

Enzyme and pathway databases

SABIO-RKP20000.
UniPathwayUPA00780; UER00768.

Family and domain databases

Gene3D3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProIPR016161. Ald_DH/histidinol_DH.
IPR016163. Ald_DH_C.
IPR016160. Ald_DH_CS.
IPR016162. Ald_DH_N.
IPR015590. Aldehyde_DH_dom.
[Graphical view]
PfamPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMSSF53720. SSF53720. 1 hit.
PROSITEPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP20000.
NextBio20868609.

Entry information

Entry nameALDH2_BOVIN
AccessionPrimary (citable) accession number: P20000
Secondary accession number(s): Q1LZC6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1991
Last sequence update: July 1, 2008
Last modified: February 19, 2014
This is version 111 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways