Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-10090-01166
Entry Name
UniProt Accession
Theoretical PI
7.53
Molecular Weight
56537.54
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Aldehyde dehydrogenase, mitochondrial
Protein Synonyms/Alias
1.2.1.3; AHD-M1; ALDH class 2; ALDH-E2; ALDHI;
Gene Name
Aldh2
Gene Synonyms/Alias
Ahd-1; Ahd1;
Created Date
01-FEB-1996
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
320
Canonical
LFFNQGQCCCAGSRT
[1]
S-Palmitoylation
321
Canonical
FFNQGQCCCAGSRTF
[1]
S-Palmitoylation
322
Canonical
FNQGQCCCAGSRTFV
[1]
S-Palmitoylation
Organism
Mus musculus (Mouse)
NCBI Taxa ID
10090
Reference
[1] Predicted from GPS-Lipid
Functional Description
Is capable of converting retinaldehyde to retinoic acid.
Sequence Annotation
Nucleotide-binding: 264 269 NAD.
Active site: 287 287 Proton acceptor.
Active site: 321 321 Nucleophile.
Functional site: 188 188 Transition state stabilizer.
Modified residue: 20 20 N-acetylserine.
Modified residue: 54 54 N6-acetyllysine.
Modified residue: 75 75 N6-acetyllysine.
Modified residue: 80 80 N6-acetyllysine.
Modified residue: 161 161 N6-acetyllysine.
Modified residue: 370 370 N6-acetyllysine.
Modified residue: 377 377 N6-acetyllysine.
Modified residue: 385 385 N6-acetyllysine.
Modified residue: 409 409 N6-acetyllysine.
Modified residue: 428 428 N6-acetyllysine.
Modified residue: 430 430 N6-acetyllysine.
Modified residue: 443 443 N6-acetyllysine.
Modified residue: 453 453 N6-acetyllysine.
Protein Length
519 AA.
Protein Sequence
(Canonical)
MLRAALTTVR RGPRLSRLLS AAATSAVPAP NHQPEVFCNQ IFINNEWHDA VSRKTFPTVN  60
PSTGEVICQV AEGNKEDVDK AVKAARAAFQ LGSPWRRMDA SDRGRLLYRL ADLIERDRTY  120
LAALETLDNG KPYVISYLVD LDMVLKCLRY YAGWADKYHG KTIPIDGDFF SYTRHEPVGV  180
CGQIIPWNFP LLMQAWKLGP ALATGNVVVM KVAEQTPLTA LYVANLIKEA GFPPGVVNIV  240
PGFGPTAGAA IASHEGVDKV AFTGSTEVGH LIQVAAGSSN LKRVTLELGG KSPNIIMSDA  300
DMDWAVEQAH FALFFNQGQC CCAGSRTFVQ ENVYDEFVER SVARAKSRVV GNPFDSRTEQ  360
GPQVDETQFK KILGYIKSGQ QEGAKLLCGG GAAADRGYFI QPTVFGDVKD GMTIAKEEIF  420
GPVMQILKFK TIEEVVGRAN DSKYGLAAAV FTKDLDKANY LSQALQAGTV WINCYDVFGA  480
QSPFGGYKMS GSGRELGEYG LQAYTEVKTV TVKVPQKNS                         519
FASTA
(Canonical)
>LipidDB-10090-01166|P47738
MLRAALTTVRRGPRLSRLLSAAATSAVPAPNHQPEVFCNQIFINNEWHDAVSRKTFPTVN
PSTGEVICQVAEGNKEDVDKAVKAARAAFQLGSPWRRMDASDRGRLLYRLADLIERDRTY
LAALETLDNGKPYVISYLVDLDMVLKCLRYYAGWADKYHGKTIPIDGDFFSYTRHEPVGV
CGQIIPWNFPLLMQAWKLGPALATGNVVVMKVAEQTPLTALYVANLIKEAGFPPGVVNIV
PGFGPTAGAAIASHEGVDKVAFTGSTEVGHLIQVAAGSSNLKRVTLELGGKSPNIIMSDA
DMDWAVEQAHFALFFNQGQCCCAGSRTFVQENVYDEFVERSVARAKSRVVGNPFDSRTEQ
GPQVDETQFKKILGYIKSGQQEGAKLLCGGGAAADRGYFIQPTVFGDVKDGMTIAKEEIF
GPVMQILKFKTIEEVVGRANDSKYGLAAAVFTKDLDKANYLSQALQAGTVWINCYDVFGA
QSPFGGYKMSGSGRELGEYGLQAYTEVKTVTVKVPQKNS
Gene Ontology
GO:0005739; C:mitochondrion; IDA:MGI
GO:0004029; F:aldehyde dehydrogenase (NAD) activity; IEA:UniProtKB-EC
GO:0006068; P:ethanol catabolic process; IEA:UniProtKB-UniPathway
Interpro
InterPro; IPR016161; Ald_DH/histidinol_DH
InterPro; IPR016163; Ald_DH_C
InterPro; IPR016160; Ald_DH_CS_CYS
InterPro; IPR029510; Ald_DH_CS_GLU
InterPro; IPR016162; Ald_DH_N
InterPro; IPR015590; Aldehyde_DH_dom
Pfam
Pfam; PF00171; Aldedh;
SMART
PROSITE
PROSITE; PS00070; ALDEHYDE_DEHYDR_CYS;
PROSITE; PS00687; ALDEHYDE_DEHYDR_GLU;
PRINTS