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Q25417 (ALDH2_LEITA) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 68. 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
P51
Gene names
Name:ALDH2
OrganismLeishmania tarentolae (Sauroleishmania tarentolae)
Taxonomic identifier5689 [NCBI]
Taxonomic lineageEukaryotaEuglenozoaKinetoplastidaTrypanosomatidaeLeishmaniinaeLeishmanializard Leishmania

Protein attributes

Sequence length498 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Could have an RNA-binding activity in addition of its catalytic role.

Catalytic activity

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

Pathway

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

Subcellular location

Mitochondrion.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Ontologies

Keywords
   Cellular componentMitochondrion
   DomainTransit peptide
   LigandNAD
RNA-binding
   Molecular functionOxidoreductase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processethanol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

   Cellular_componentmitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionRNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

aldehyde 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 – 99Mitochondrion Ref.1
Chain10 – 498489Aldehyde dehydrogenase, mitochondrial
PRO_0000007171

Regions

Nucleotide binding242 – 2476NAD By similarity

Sites

Active site2651Proton acceptor By similarity
Active site2991Nucleophile By similarity
Site1661Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q25417 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 618D55F6ED5547EC

FASTA49854,252
        10         20         30         40         50         60 
MLRATLARLE MAPKVTHIQE KLLINGKFVP AVSGKTFEVV NPADEKVIAN VAEAEKADVD 

        70         80         90        100        110        120 
LAVKAARHAF ESFRMTDCQW RRNLMLRLAD ILEKNSKEMA ALESLDNGKP YEVALNVDVA 

       130        140        150        160        170        180 
LSVECFRYCA GLADKVNGTV PPRSGNFLGI VKRQPIGVCG QIIPWNFPLL MAAFKLSPAL 

       190        200        210        220        230        240 
AMGNTVVLKP AEQTPLTAVR LGEMVMEAGY PDGVLNILPG FGATAGSEIA RHMDVDKIAF 

       250        260        270        280        290        300 
TGSTAVGHQV MQMAAETNLK KVSLELGGKS ALIVCEDADL EEAAEVATTR VYFNTGQVCT 

       310        320        330        340        350        360 
ASSRIYVHES VYDEFVSRLR KNAEARKVGP GNDTGNNMGP LVSKKQHERV LGYIEDGVKA 

       370        380        390        400        410        420 
GATVVTGGKK IGDKGYFVQP TIFSDVKEDM RICKEEIFGP VTCVMKYKDM DEVVKRANDS 

       430        440        450        460        470        480 
IYGLAAGICT RSMDTALRYS TYLNAGTVWV NTWNNFCPSM PFGGFKQSGI GRELGKEVVD 

       490 
MYTEPKAIHF ASRSIVKP 

« Hide

References

[1]"Characterization of two nuclear-encoded protein components of mitochondrial ribonucleoprotein complexes from Leishmania tarentolae."
Bringaud F., Peris M., Zen K.H., Simpson L.
Mol. Biochem. Parasitol. 71:65-79(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 10-31.
Strain: UC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Z31698 Genomic DNA. Translation: CAA83503.1.
PIRS43184.

3D structure databases

ProteinModelPortalQ25417.
ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ25417.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

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_LEITA
AccessionPrimary (citable) accession number: Q25417
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: March 19, 2014
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways