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P12762 (ALDH2_HORSE) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismEquus caballus (Horse) [Reference proteome]
Taxonomic identifier9796 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaPerissodactylaEquidaeEquus

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
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
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete 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

Chain1 – 500500Aldehyde dehydrogenase, mitochondrial
PRO_0000056467

Regions

Nucleotide binding245 – 2506NAD By similarity

Sites

Active site2681Proton acceptor By similarity
Active site3021Nucleophile By similarity
Site1691Transition state stabilizer By similarity

Amino acid modifications

Modified residue351N6-acetyllysine By similarity
Modified residue561N6-acetyllysine By similarity
Modified residue1421N6-acetyllysine By similarity
Modified residue3581N6-acetyllysine By similarity
Modified residue3661N6-acetyllysine By similarity
Modified residue4091N6-acetyllysine By similarity
Modified residue4111N6-acetyllysine By similarity
Modified residue4241N6-acetyllysine By similarity
Modified residue4341N6-acetyllysine By similarity

Natural variations

Natural variant11A → L.
Natural variant11A → S.

Sequences

Sequence LengthMass (Da)Tools
P12762 [UniParc].

Last modified October 1, 1989. Version 1.
Checksum: 7F95364A73383B24

FASTA50054,166
        10         20         30         40         50         60 
AAAATQAVPA PNQQPEVFYN QIFINNEWHD AVSKKTFPTV NPSTGEVICQ VAAGDKEDVD 

        70         80         90        100        110        120 
RAVKAARAAF QLGSPWRRMD ASDRGRLLNR LADLIERDRT YLAALETLDN GKPYVISYLV 

       130        140        150        160        170        180 
DLDMVLKCLR YYAGWADKYH GKTIPIDGDF FSYTRHEPVG VCGQIIPWNF PLLMQAAKLG 

       190        200        210        220        230        240 
PALATGNVVV MKVAEQTPLT ALYVANLTKE AGFPPGVVNV VPGFGPTAGA AIASHEDVDK 

       250        260        270        280        290        300 
VAFTGSTEVG HLIQVAAGRS NLKKVTLELG GKSPNIIVSD ADMDWAVEQA HFALFFNQGQ 

       310        320        330        340        350        360 
CCGAGSRTFV QEDVYAEFVE RSVARAKSRV VGNPFDSQTE QGPQVDETQF NKVLGYIKSG 

       370        380        390        400        410        420 
KEEGAKLLCG GGAAADRGYF IQPTVFGDVQ DGMTIAKEEI FGPVMQILKF KTIEEVVGRA 

       430        440        450        460        470        480 
NNSKYGLAAA VFTKDLDKAN YLSQALQAGT VWINCYDVFG AQSPFGGYKM SGNGRELGEY 

       490        500 
GLQAYTEVKT VTIKVPQKNS 

« Hide

References

[1]"Mitochondrial aldehyde dehydrogenase from horse liver. Correlations of the same species variants for both the cytosolic and the mitochondrial forms of an enzyme."
Johansson J., von Bahr-Lindstroem H., Jeck R., Woenckhaus C., Joernvall H.
Eur. J. Biochem. 172:527-533(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRS00364.

3D structure databases

ProteinModelPortalP12762.
SMRP12762. Positions 6-500.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9796.ENSECAP00000015826.

Proteomic databases

PRIDEP12762.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGCOG1012.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidP12762.

Enzyme and pathway databases

SABIO-RKP12762.
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_CYS.
IPR029510. Ald_DH_CS_GLU.
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...

Entry information

Entry nameALDH2_HORSE
AccessionPrimary (citable) accession number: P12762
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1989
Last sequence update: October 1, 1989
Last modified: June 11, 2014
This is version 88 of the entry and version 1 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

PATHWAY comments

Index of metabolic and biosynthesis pathways