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P81178 (ALDH2_MESAU) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 71. 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
ALDH1
Gene names
Name:ALDH2
OrganismMesocricetus auratus (Golden hamster)
Taxonomic identifier10036 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaCricetidaeCricetinaeMesocricetus

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 termDirect protein sequencing
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_0000056468

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 residue611N6-acetyllysine By similarity
Modified residue1421N6-acetyllysine By similarity
Modified residue3511N6-acetyllysine By similarity
Modified residue3581N6-acetyllysine By similarity
Modified residue3661N6-acetyllysine By similarity
Modified residue3901N6-acetyllysine By similarity
Modified residue4091N6-acetyllysine By similarity
Modified residue4111N6-acetyllysine By similarity
Modified residue4241N6-acetyllysine By similarity
Modified residue4341N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
P81178 [UniParc].

Last modified July 15, 1998. Version 1.
Checksum: 8B81886AB04F493F

FASTA50054,334
        10         20         30         40         50         60 
SAAATSAVPA PNQQPEVFCN QIFINNEWHD AVSKKTFPTV NPSTGEVICQ VAEGSKEDVD 

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

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

       190        200        210        220        230        240 
PALATGNVVV MKVAEQTPLT ALYVANLIKE AGFPPGVVNI VPGFGPTAGA AIASHEDVDK 

       250        260        270        280        290        300 
VAFTGSTEVG HLIQVAAGSS NLKRVTLELG GKSPNIIMSD ADMDWAVEQA HFALFFNQGQ 

       310        320        330        340        350        360 
CCCAGSRTFV QEDVYDEFVE RSVARAKSRV VGNPFDSRTE QGPQVDETQF KKILGYIKSG 

       370        380        390        400        410        420 
QQEGAKLLCG GGAAADRGYF IQPTVFGDVK DGMTIAKEEI FGPVMQILKF KTIEEVVGRA 

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

       490        500 
GLQAYTEVKT VTIKVPQKNS 

« Hide

References

[1]"Class 2 aldehyde dehydrogenase. Characterization of the hamster enzyme, sensitive to daidzin and conserved within the family of multiple forms."
Hjelmqvist L., Lundgren R., Norin A., Joernvall H., Vallee B., Klyosov A., Keung W.M.
FEBS Lett. 416:99-102(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Liver.
[2]"Glucose-regulated protein precursor (GRP78) and tumor rejection antigen (GP96) are unique to hamster caput epididymal spermatozoa."
Kameshwari D.B., Bhande S., Sundaram C.S., Kota V., Siva A.B., Shivaji S.
Asian J. Androl. 12:344-355(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.

Cross-references

3D structure databases

ProteinModelPortalP81178.
SMRP81178. Positions 7-500.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEP81178.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG000097.

Enzyme and pathway databases

SABIO-RKP81178.
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...

Entry information

Entry nameALDH2_MESAU
AccessionPrimary (citable) accession number: P81178
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1998
Last sequence update: July 15, 1998
Last modified: November 13, 2013
This is version 71 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