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Q9JLJ2

- AL9A1_MOUSE

UniProt

Q9JLJ2 - AL9A1_MOUSE

Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

Aldh9a1

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
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    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: UniProtKB-EC
    2. amine binding Source: Ensembl
    3. aminobutyraldehyde dehydrogenase activity Source: Ensembl
    4. NAD binding Source: Ensembl
    5. 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: Ensembl
    4. kidney development Source: Ensembl
    5. liver development Source: Ensembl
    6. neurotransmitter biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    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: Unplaced

    Organism-specific databases

    MGIiMGI:1861622. Aldh9a1.

    Subcellular locationi

    Cytoplasm By similarity

    GO - Cellular componenti

    1. cytosol Source: MGI
    2. mitochondrion Source: MGI
    3. plasma membrane Source: Ensembl

    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

    ArrayExpressiQ9JLJ2.
    BgeeiQ9JLJ2.
    CleanExiMM_ALDH9A1.
    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

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    MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGRVI ATFACSGEKE    50
    VNLAVENAKA AFKLWSKKSG LERCQVLLEA ARIIKERKDE IATVETINNG 100
    KSIFEARLDV DTCWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC 150
    VGIGAWNYPF QIACWKSAPA LACGNAMIFK PSPFTPVSAL LLAEIYTKAG 200
    APPGLFNVVQ GGAATGQFLC HHREVAKISF TGSVPTGVKI MEMSAKGVKP 250
    ITLELGGKSP LIIFSDCNME NAVKGALMAN FLTQGQVCCN GTRVFVQKEI 300
    ADKFINEVVK QTQKIKLGDP LLEDTRMGPL INAPHLERVL GFVKLAKEQG 350
    ATVLCGGEVY VPEDPKLKHG YYMTPCILTN CRDDMTCVKE EIFGPVMSIL 400
    TFGTEAEVLE RANDTTFGLA AGVFTRDIQR AHRVAAELQA GTCYINNYNV 450
    SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF 494
    Length:494
    Mass (Da):53,515
    Last modified:October 1, 2000 - v1
    Checksum:iCBB27755330E0A23
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170919 mRNA. Translation: AAF43599.1 .
    BC003297 mRNA. Translation: AAH03297.1 .
    RefSeqi NP_064377.2. NM_019993.3.
    UniGenei Mm.330055.

    3D structure databases

    ProteinModelPortali Q9JLJ2.
    SMRi Q9JLJ2. Positions 2-494.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JLJ2. 3 interactions.
    MINTi MINT-4087568.

    PTM databases

    PhosphoSitei Q9JLJ2.

    2D gel databases

    REPRODUCTION-2DPAGE Q9JLJ2.

    Proteomic databases

    MaxQBi Q9JLJ2.
    PaxDbi Q9JLJ2.
    PRIDEi Q9JLJ2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 56752.
    KEGGi mmu:56752.

    Organism-specific databases

    CTDi 223.
    MGIi MGI:1861622. Aldh9a1.

    Phylogenomic databases

    eggNOGi COG1012.
    HOVERGENi HBG000097.
    InParanoidi Q9JLJ2.
    KOi K00149.
    PhylomeDBi Q9JLJ2.

    Enzyme and pathway databases

    UniPathwayi UPA00118 .

    Miscellaneous databases

    NextBioi 313278.
    PROi Q9JLJ2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9JLJ2.
    Bgeei Q9JLJ2.
    CleanExi MM_ALDH9A1.
    Genevestigatori Q9JLJ2.

    Family and domain databases

    Gene3Di 3.40.309.10. 1 hit.
    3.40.605.10. 1 hit.
    InterProi IPR016161. 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 ]
    Pfami PF00171. Aldedh. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53720. SSF53720. 1 hit.
    PROSITEi PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit.
    PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 108 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