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Q9JLJ2 (AL9A1_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 105. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
4-trimethylaminobutyraldehyde dehydrogenase

Short name=TMABADH
EC=1.2.1.47
Alternative name(s):
Aldehyde dehydrogenase family 9 member A1
EC=1.2.1.3
Gene names
Name:Aldh9a1
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length494 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine By similarity.

Catalytic activity

4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH.

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

Pathway

Amine and polyamine biosynthesis; carnitine biosynthesis.

Subunit structure

Homotetramer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the aldehyde dehydrogenase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 4944934-trimethylaminobutyraldehyde dehydrogenase
PRO_0000056486

Regions

Nucleotide binding232 – 2376NAD By similarity

Sites

Active site2541 Potential
Active site2881 Potential

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue301N6-acetyllysine; alternate Ref.5
Modified residue301N6-succinyllysine; alternate Ref.4
Modified residue591N6-succinyllysine Ref.4
Modified residue2981N6-acetyllysine Ref.5
Modified residue3031N6-acetyllysine; alternate Ref.5
Modified residue3031N6-succinyllysine; alternate Ref.4
Modified residue3441N6-acetyllysine Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q9JLJ2 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: CBB27755330E0A23

FASTA49453,515
        10         20         30         40         50         60 
MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGRVI ATFACSGEKE VNLAVENAKA 

        70         80         90        100        110        120 
AFKLWSKKSG LERCQVLLEA ARIIKERKDE IATVETINNG KSIFEARLDV DTCWQCLEYY 

       130        140        150        160        170        180 
AGLAASMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QIACWKSAPA LACGNAMIFK 

       190        200        210        220        230        240 
PSPFTPVSAL LLAEIYTKAG APPGLFNVVQ GGAATGQFLC HHREVAKISF TGSVPTGVKI 

       250        260        270        280        290        300 
MEMSAKGVKP ITLELGGKSP LIIFSDCNME NAVKGALMAN FLTQGQVCCN GTRVFVQKEI 

       310        320        330        340        350        360 
ADKFINEVVK QTQKIKLGDP LLEDTRMGPL INAPHLERVL GFVKLAKEQG ATVLCGGEVY 

       370        380        390        400        410        420 
VPEDPKLKHG YYMTPCILTN CRDDMTCVKE EIFGPVMSIL TFGTEAEVLE RANDTTFGLA 

       430        440        450        460        470        480 
AGVFTRDIQR AHRVAAELQA GTCYINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL 

       490 
KTVCVEMGDV ESAF 

« Hide

References

« Hide 'large scale' references
[1]"Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis."
Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A.
J. Biol. Chem. 275:7390-7394(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Liver.
[2]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Strain: FVB/N.
Tissue: Mammary tumor.
[3]Lubec G., Sunyer B., Chen W.-Q.
Submitted (JAN-2009) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 39-59; 74-82; 88-101; 228-239; 247-274; 317-338; 348-366; 412-426 AND 472-494, IDENTIFICATION BY MASS SPECTROMETRY.
Strain: OF1.
Tissue: Hippocampus.
[4]"SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: SUCCINYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-59 AND LYS-303, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways."
Rardin M.J., Newman J.C., Held J.M., Cusack M.P., Sorensen D.J., Li B., Schilling B., Mooney S.D., Kahn C.R., Verdin E., Gibson B.W.
Proc. Natl. Acad. Sci. U.S.A. 110:6601-6606(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-30; LYS-298; LYS-303 AND LYS-344, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170919 mRNA. Translation: AAF43599.1.
BC003297 mRNA. Translation: AAH03297.1.
RefSeqNP_064377.2. NM_019993.3.
UniGeneMm.330055.

3D structure databases

ProteinModelPortalQ9JLJ2.
SMRQ9JLJ2. Positions 2-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JLJ2. 3 interactions.
MINTMINT-4087568.

PTM databases

PhosphoSiteQ9JLJ2.

2D gel databases

REPRODUCTION-2DPAGEQ9JLJ2.

Proteomic databases

PaxDbQ9JLJ2.
PRIDEQ9JLJ2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID56752.
KEGGmmu:56752.

Organism-specific databases

CTD223.
MGIMGI:1861622. Aldh9a1.

Phylogenomic databases

eggNOGCOG1012.
HOVERGENHBG000097.
InParanoidQ9JLJ2.
KOK00149.
PhylomeDBQ9JLJ2.

Enzyme and pathway databases

UniPathwayUPA00118.

Gene expression databases

ArrayExpressQ9JLJ2.
BgeeQ9JLJ2.
CleanExMM_ALDH9A1.
GenevestigatorQ9JLJ2.

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...

Other

NextBio313278.
PROQ9JLJ2.
SOURCESearch...

Entry information

Entry nameAL9A1_MOUSE
AccessionPrimary (citable) accession number: Q9JLJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 105 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

PATHWAY comments

Index of metabolic and biosynthesis pathways

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot