Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P13601 (AL1A7_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 103. 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, cytosolic 1

EC=1.2.1.3
Alternative name(s):
ALDH class 1
ALDH-E1
ALHDII
Aldehyde dehydrogenase family 1 member A7
Aldehyde dehydrogenase phenobarbital-inducible
Gene names
Name:Aldh1a7
Synonyms:Aldh-pb, Aldh1, Aldh1a4
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

Protein attributes

Sequence length501 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Can oxidize benzaldehyde, propionaldehyde and acetaldehyde. No detectable activity with retinal. Ref.2

Catalytic activity

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

Pathway

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

Subunit structure

Homotetramer. Ref.2

Subcellular location

Cytoplasm.

Tissue specificity

Very low levels in lung and liver. Ref.2

Induction

By phenobarbital.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Biophysicochemical properties

Kinetic parameters:

The highest catalytic efficiency is observed with benzaldehyde as substrate. No activity with retinal.

KM=2.4 mM for acetaldehyde Ref.2

KM=1.6 mM for propionaldehyde

KM=4.7 µM for benzaldehyde

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 501501Aldehyde dehydrogenase, cytosolic 1
PRO_0000056426

Regions

Nucleotide binding246 – 2516NAD By similarity

Sites

Active site2691Proton acceptor By similarity
Active site3031Nucleophile By similarity
Site1701Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
P13601 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: E6806A1AF736AF1F

FASTA50154,560
        10         20         30         40         50         60 
MSSPAQPAVP APLANLKIQH TKIFINNEWH NSLNGKKFPV INPATEEVIC HVEEGDKADV 

        70         80         90        100        110        120 
DKAVKAARQA FQIGSPWRTM DASERGCLLN KLADLMERDR VLLATMESMN AGKIFTHAYL 

       130        140        150        160        170        180 
LDTEVSIKAL KYFAGWADKI HGQTIPSDGD VFTYTRREPI GVCGQIIPWN GPLILFIWKI 

       190        200        210        220        230        240 
GAALSCGNTV IVKPAEQTPL TALYMASLIK EAGFPPGVVN VVPGYGSTAG AAISSHMDID 

       250        260        270        280        290        300 
KVSFTGSTEV GKLIKEAAGK SNLKRVTLEL GGKSPCIVFA DADLDSAVEF AHQGVFFHQG 

       310        320        330        340        350        360 
QICVAASRLF VEESIYDEFV RRSVERAKKY VLGNPLDSGI SQGPQIDKEQ HAKILDLIES 

       370        380        390        400        410        420 
GKKEGAKLEC GGGRWGNKGF FVQPTVFSNV TDEMRIAKEE IFGPVQQIMK FKSIDEVIKR 

       430        440        450        460        470        480 
ANNTPYGLAA GVFTKDLDRA ITVSSALQAG TVWVNCYLTL SVQCPFGGFK MSGNGREMGE 

       490        500 
QGVYEYTELK TVAMKISQKN S 

« Hide

References

[1]"Phenobarbital-inducible aldehyde dehydrogenase in the rat. cDNA sequence and regulation of the mRNA by phenobarbital in responsive rats."
Dunn T.J., Koleske A.J., Lindahl R., Pitot H.C.
J. Biol. Chem. 264:13057-13065(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Rat liver constitutive and phenobarbital-inducible cytosolic aldehyde dehydrogenases are highly homologous proteins that function as distinct isozymes."
Kathmann E.C., Naylor S., Lipsky J.J.
Biochemistry 39:11170-11176(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M23995 mRNA. Translation: AAA40718.1.
PIRA32616.
RefSeqNP_058968.14. NM_017272.15.
UniGeneRn.74044.

3D structure databases

ProteinModelPortalP13601.
SMRP13601. Positions 9-501.
ModBaseSearch...
MobiDBSearch...

Chemistry

BindingDBP13601.
ChEMBLCHEMBL5354.

Proteomic databases

PRIDEP13601.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCRGD:620252. rat.

Organism-specific databases

RGD620252. Aldh1a7.

Phylogenomic databases

HOVERGENHBG000097.
PhylomeDBP13601.

Enzyme and pathway databases

SABIO-RKP13601.
UniPathwayUPA00780; UER00768.

Gene expression databases

GenevestigatorP13601.

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 nameAL1A7_RAT
AccessionPrimary (citable) accession number: P13601
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1990
Last sequence update: January 23, 2007
Last modified: June 11, 2014
This is version 103 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

PATHWAY comments

Index of metabolic and biosynthesis pathways