Reviewed, UniProtKB/Swiss-Prot P13601 (AL1A7_RAT)

Names and origin

Protein names

Recommended name:
    Aldehyde dehydrogenase, cytosolic 1
    EC=1.2.1.3
Alternative name(s):
    ALDH class 1
    ALHDII
    ALDH-E1
    Aldehyde dehydrogenase family 1 member A7
    Aldehyde dehydrogenase phenobarbital-inducible

Gene names

Name:	Aldh1a7
Synonyms:	Aldh-pb, Aldh1, Aldh1a4

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length	501 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Can oxidize benzaldehyde, propionaldehyde and acetaldehyde. No detectable activity with retinal.
Catalytic activity	An aldehyde + NAD(+) + H(2)O = an acid + NADH.
Pathway	Alcohol metabolism; ethanol degradation; acetate from ethanol: step 2/2.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm.
Tissue specificity	Very low levels in lung and liver.
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 KM=1.6 mM for propionaldehyde KM=4.7 µM for benzaldehyde

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
Gene Ontology (GO)
Biological process	oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	aldehyde dehydrogenase (NAD) activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 501	500	Aldehyde dehydrogenase, cytosolic 1		PRO_0000056426
Regions
	Nucleotide binding	246 – 251	6	NAD By similarity
Sites
	Active site	269	1	Proton acceptor By similarity
	Active site	303	1	Nucleophile By similarity
	Site	170	1	Transition state stabilizer By similarity

Sequences

	Sequence		Length	Mass (Da)
	P13601-1 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: E6806A1AF736AF1F	FASTA	501	54,560
	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

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: 2753900] [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: 10998257] [Abstract] Cited for: FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, TISSUE SPECIFICITY.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M23995 mRNA. Translation: AAA40718.1.
PIR	A32616.
RefSeq	NP_058968.14.
UniGene	Rn.74044
3D structure databases
HSSP	HSSP built from PDB template 1BXS based on UniProtKB P51977.
ModBase	Search...
Genome annotation databases
KEGG	rno:29651.
Organism-specific databases
RGD	620252. Aldh1a7.
Phylogenomic databases
HOVERGEN	P13601.
Family and domain databases
InterPro	IPR016160. Ald_DHase_CS. IPR016162. Ald_DHase_N. IPR015590. Aldehyde_DHase. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AL1A7_RAT

Accession

Primary (citable) accession number: P13601

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	January 23, 2007
Last modified:	November 4, 2008
This is version 68 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)