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Q5RF00 (ALDH2_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | 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
Gene names
Name:ALDH2
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length517 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Is capable of converting retinaldehyde to retinoic acid By similarity.

Catalytic activity

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

Subunit structure

Homotetramer By similarity.

Subcellular location

Mitochondrion matrix By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
   Molecular functionOxidoreductase
   PTMAcetylation
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   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 – 1717Mitochondrion By similarity
Chain18 – 517500Aldehyde dehydrogenase, mitochondrial
PRO_0000312493

Regions

Nucleotide binding262 – 2676NAD By similarity

Sites

Active site2851Proton acceptor By similarity
Active site3191Nucleophile By similarity
Site1861Transition state stabilizer By similarity

Amino acid modifications

Modified residue521N6-acetyllysine By similarity
Modified residue731N6-acetyllysine By similarity
Modified residue781N6-acetyllysine By similarity
Modified residue1591N6-acetyllysine By similarity
Modified residue3681N6-acetyllysine By similarity
Modified residue3831N6-acetyllysine By similarity
Modified residue4261N6-acetyllysine By similarity
Modified residue4281N6-acetyllysine By similarity
Modified residue4511N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RF00 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: E8F74D4CFA27220E

FASTA51756,380
        10         20         30         40         50         60 
MLRAAARFGP RLGRRLLSAA ATQAVPAPNQ QPEVFCNQIF INNEWHDAVS RKTFPTVNPS 

        70         80         90        100        110        120 
TGEVICQVAE GDKEDVDKAV KAARAAFQLG SPWRRMDASH RGRLLNRLAD LIERDRTYLA 

       130        140        150        160        170        180 
ALETLDNGKP YVISYLVDLD MVLKCLRYYA GWADKYHGKT IPIDGDFFSY TRHEPVGVCG 

       190        200        210        220        230        240 
QIIPWNFPLL MQAWKLGPAL ATGNVVVMKV AEQTPLTALY VANLIKEAGF PPGVVNIVPG 

       250        260        270        280        290        300 
FGPTAGAAIA SHEDVDKVAF TGSTEIGRVI QVAAGSSNLK RVTLELGGKS PNIIMSDADM 

       310        320        330        340        350        360 
DWAVEQAHFA LFFNQGQCCC AGSRTFVQED IYDEFVERSV ARAKSRVVGN PFDSKTEQGP 

       370        380        390        400        410        420 
QVDETQFKKI LGYINTGKQE GAKLLCGGGI AADRGYFIQP TVFGDVQDGM TIAKEEIFGP 

       430        440        450        460        470        480 
VMQILKFKTI EEVVGRANNS TYGLAAAVFT KDLDKANYLS QALQAGTVWV NCYNVFGAQS 

       490        500        510 
PFGGYKMSGS GRELGEYGLQ AYTEVKTVTV KVPQKNS 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR857362 mRNA. Translation: CAH89657.1.
RefSeqNP_001124747.1. NM_001131275.1.
UniGenePab.6233.

3D structure databases

ProteinModelPortalQ5RF00.
SMRQ5RF00. Positions 23-517.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ5RF00.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171596.
KEGGpon:100171596.

Organism-specific databases

CTD217.

Phylogenomic databases

HOVERGENHBG000097.
KOK00128.

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_PONAB
AccessionPrimary (citable) accession number: Q5RF00
Entry history
Integrated into UniProtKB/Swiss-Prot: December 4, 2007
Last sequence update: December 21, 2004
Last modified: November 13, 2013
This is version 52 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