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Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

Aldh9a1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine.By similarity

Catalytic activityi

4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH.
An aldehyde + NAD+ + H2O = a carboxylate + NADH.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei254 – 2541Sequence Analysis
Active sitei288 – 2881Sequence Analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi232 – 2376NADBy similarity

GO - Molecular functioni

  1. 4-trimethylammoniobutyraldehyde dehydrogenase activity Source: GO_Central
  2. aldehyde dehydrogenase (NAD) activity Source: MGI
  3. amine binding Source: Ensembl
  4. aminobutyraldehyde dehydrogenase activity Source: MGI
  5. NAD binding Source: Ensembl
  6. oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Source: MGI

GO - Biological processi

  1. carnitine biosynthetic process Source: UniProtKB-UniPathway
  2. carnitine metabolic process Source: MGI
  3. cellular aldehyde metabolic process Source: MGI
  4. kidney development Source: Ensembl
  5. liver development Source: Ensembl
  6. neurotransmitter biosynthetic process Source: MGI
  7. oxidation-reduction process Source: MGI
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BRENDAi1.2.1.47. 3474.
ReactomeiREACT_354893. Carnitine synthesis.
UniPathwayiUPA00118.

Names & Taxonomyi

Protein namesi
Recommended name:
4-trimethylaminobutyraldehyde dehydrogenase (EC:1.2.1.47)
Short name:
TMABADH
Alternative name(s):
Aldehyde dehydrogenase family 9 member A1 (EC:1.2.1.3)
Gene namesi
Name:Aldh9a1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589 Componenti: Unplaced

Organism-specific databases

MGIiMGI:1861622. Aldh9a1.

Subcellular locationi

  1. Cytoplasm By similarity

GO - Cellular componenti

  1. cytosol Source: MGI
  2. extracellular vesicular exosome Source: MGI
  3. mitochondrion Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 4944934-trimethylaminobutyraldehyde dehydrogenasePRO_0000056486Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei30 – 301N6-acetyllysine; alternate1 Publication
Modified residuei30 – 301N6-succinyllysine; alternate1 Publication
Modified residuei59 – 591N6-succinyllysine1 Publication
Modified residuei298 – 2981N6-acetyllysine1 Publication
Modified residuei303 – 3031N6-acetyllysine; alternate1 Publication
Modified residuei303 – 3031N6-succinyllysine; alternate1 Publication
Modified residuei344 – 3441N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9JLJ2.
PaxDbiQ9JLJ2.
PRIDEiQ9JLJ2.

2D gel databases

REPRODUCTION-2DPAGEQ9JLJ2.

PTM databases

PhosphoSiteiQ9JLJ2.

Expressioni

Gene expression databases

BgeeiQ9JLJ2.
CleanExiMM_ALDH9A1.
ExpressionAtlasiQ9JLJ2. baseline and differential.
GenevestigatoriQ9JLJ2.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9JLJ2. 3 interactions.
MINTiMINT-4087568.

Structurei

3D structure databases

ProteinModelPortaliQ9JLJ2.
SMRiQ9JLJ2. Positions 2-494.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the aldehyde dehydrogenase family.Curated

Phylogenomic databases

eggNOGiCOG1012.
HOVERGENiHBG000097.
InParanoidiQ9JLJ2.
KOiK00149.
PhylomeDBiQ9JLJ2.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q9JLJ2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGRVI ATFACSGEKE
60 70 80 90 100
VNLAVENAKA AFKLWSKKSG LERCQVLLEA ARIIKERKDE IATVETINNG
110 120 130 140 150
KSIFEARLDV DTCWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC
160 170 180 190 200
VGIGAWNYPF QIACWKSAPA LACGNAMIFK PSPFTPVSAL LLAEIYTKAG
210 220 230 240 250
APPGLFNVVQ GGAATGQFLC HHREVAKISF TGSVPTGVKI MEMSAKGVKP
260 270 280 290 300
ITLELGGKSP LIIFSDCNME NAVKGALMAN FLTQGQVCCN GTRVFVQKEI
310 320 330 340 350
ADKFINEVVK QTQKIKLGDP LLEDTRMGPL INAPHLERVL GFVKLAKEQG
360 370 380 390 400
ATVLCGGEVY VPEDPKLKHG YYMTPCILTN CRDDMTCVKE EIFGPVMSIL
410 420 430 440 450
TFGTEAEVLE RANDTTFGLA AGVFTRDIQR AHRVAAELQA GTCYINNYNV
460 470 480 490
SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF
Length:494
Mass (Da):53,515
Last modified:October 1, 2000 - v1
Checksum:iCBB27755330E0A23
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170919 mRNA. Translation: AAF43599.1.
BC003297 mRNA. Translation: AAH03297.1.
RefSeqiNP_064377.2. NM_019993.3.
UniGeneiMm.330055.

Genome annotation databases

GeneIDi56752.
KEGGimmu:56752.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170919 mRNA. Translation: AAF43599.1.
BC003297 mRNA. Translation: AAH03297.1.
RefSeqiNP_064377.2. NM_019993.3.
UniGeneiMm.330055.

3D structure databases

ProteinModelPortaliQ9JLJ2.
SMRiQ9JLJ2. Positions 2-494.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9JLJ2. 3 interactions.
MINTiMINT-4087568.

PTM databases

PhosphoSiteiQ9JLJ2.

2D gel databases

REPRODUCTION-2DPAGEQ9JLJ2.

Proteomic databases

MaxQBiQ9JLJ2.
PaxDbiQ9JLJ2.
PRIDEiQ9JLJ2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi56752.
KEGGimmu:56752.

Organism-specific databases

CTDi223.
MGIiMGI:1861622. Aldh9a1.

Phylogenomic databases

eggNOGiCOG1012.
HOVERGENiHBG000097.
InParanoidiQ9JLJ2.
KOiK00149.
PhylomeDBiQ9JLJ2.

Enzyme and pathway databases

UniPathwayiUPA00118.
BRENDAi1.2.1.47. 3474.
ReactomeiREACT_354893. Carnitine synthesis.

Miscellaneous databases

NextBioi313278.
PROiQ9JLJ2.
SOURCEiSearch...

Gene expression databases

BgeeiQ9JLJ2.
CleanExiMM_ALDH9A1.
ExpressionAtlasiQ9JLJ2. baseline and differential.
GenevestigatoriQ9JLJ2.

Family and domain databases

Gene3Di3.40.309.10. 1 hit.
3.40.605.10. 1 hit.
InterProiIPR016161. 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]
PfamiPF00171. Aldedh. 1 hit.
[Graphical view]
SUPFAMiSSF53720. SSF53720. 1 hit.
PROSITEiPS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.

Entry informationi

Entry nameiAL9A1_MOUSE
AccessioniPrimary (citable) accession number: Q9JLJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: April 1, 2015
This is version 114 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.