Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9JLJ3

- AL9A1_RAT

UniProt

Q9JLJ3 - AL9A1_RAT

Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

Aldh9a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 98 (01 Oct 2014)
      Sequence version 1 (01 Oct 2000)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine.1 Publication

    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: RGD
    2. aldehyde dehydrogenase (NAD) activity Source: RGD
    3. amine binding Source: RGD
    4. aminobutyraldehyde dehydrogenase activity Source: RGD
    5. NAD binding Source: RGD
    6. protein homodimerization activity Source: RGD

    GO - Biological processi

    1. carnitine biosynthetic process Source: RGD
    2. cellular aldehyde metabolic process Source: Ensembl
    3. kidney development Source: RGD
    4. liver development Source: RGD
    5. neurotransmitter biosynthetic process Source: Ensembl

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Ligandi

    NAD

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-14430.
    SABIO-RKQ9JLJ3.
    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
    OrganismiRattus norvegicus (Rat)
    Taxonomic identifieri10116 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
    ProteomesiUP000002494: Chromosome 13

    Organism-specific databases

    RGDi68409. Aldh9a1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: RGD
    2. mitochondrion Source: Ensembl
    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_0000056489Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylserineBy similarity
    Modified residuei30 – 301N6-acetyllysine; alternateBy similarity
    Modified residuei30 – 301N6-succinyllysine; alternateBy similarity
    Modified residuei59 – 591N6-succinyllysineBy similarity
    Modified residuei298 – 2981N6-acetyllysineBy similarity

    Keywords - PTMi

    Acetylation

    Proteomic databases

    PaxDbiQ9JLJ3.
    PRIDEiQ9JLJ3.

    PTM databases

    PhosphoSiteiQ9JLJ3.

    Expressioni

    Gene expression databases

    GenevestigatoriQ9JLJ3.

    Interactioni

    Subunit structurei

    Homotetramer.By similarity

    Protein-protein interaction databases

    IntActiQ9JLJ3. 1 interaction.
    MINTiMINT-4580055.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9JLJ3.
    SMRiQ9JLJ3. Positions 2-492.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldehyde dehydrogenase family.Curated

    Phylogenomic databases

    eggNOGiCOG1012.
    GeneTreeiENSGT00720000108597.
    HOGENOMiHOG000271505.
    HOVERGENiHBG000097.
    InParanoidiQ9JLJ3.
    KOiK00149.
    OrthoDBiEOG7327P4.
    PhylomeDBiQ9JLJ3.

    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.

    Q9JLJ3-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGREI ATFKCSGEKE    50
    VNLAVENAKA AFKIWSKKSG LERCQVLLEA ARIIKERRDE IAIMETINNG 100
    KSIFEARLDV DTSWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC 150
    LGIGAWNYPF QIACWKSAPA LACGNAMIFK PSPFTPVSAL LLAEIYTKAG 200
    APNGLFNVVQ GGAATGQFLC QHRDVAKVSF TGSVPTGMKI MEMAAKGIKP 250
    ITLELGGKSP LIIFSDCNMK NAVKGALLAN FLTQGQVCCN GTRVFVQKEI 300
    ADAFTKEVVR QTQRIKIGDP LLEDTRMGPL INAPHLERVL GFVRSAKEQG 350
    ATVLCGGEPY APEDPKLKHG YYMTPCILTN CTDDMTCVKE EIFGPVMSIL 400
    TFETEAEVLE RANDTTFGLA AGVFTRDIQR AHRVAAELQA GTCYINNYNV 450
    SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF 494
    Length:494
    Mass (Da):53,653
    Last modified:October 1, 2000 - v1
    Checksum:iE417BD52D7DF567C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti493 – 4942AF → PFENQ in AAH74019. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170918 mRNA. Translation: AAF43598.1.
    BC074019 mRNA. Translation: AAH74019.1.
    RefSeqiNP_071609.2. NM_022273.2.
    UniGeneiRn.98155.

    Genome annotation databases

    EnsembliENSRNOT00000005611; ENSRNOP00000005611; ENSRNOG00000004027.
    GeneIDi64040.
    KEGGirno:64040.
    UCSCiRGD:68409. rat.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF170918 mRNA. Translation: AAF43598.1 .
    BC074019 mRNA. Translation: AAH74019.1 .
    RefSeqi NP_071609.2. NM_022273.2.
    UniGenei Rn.98155.

    3D structure databases

    ProteinModelPortali Q9JLJ3.
    SMRi Q9JLJ3. Positions 2-492.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    IntActi Q9JLJ3. 1 interaction.
    MINTi MINT-4580055.

    PTM databases

    PhosphoSitei Q9JLJ3.

    Proteomic databases

    PaxDbi Q9JLJ3.
    PRIDEi Q9JLJ3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSRNOT00000005611 ; ENSRNOP00000005611 ; ENSRNOG00000004027 .
    GeneIDi 64040.
    KEGGi rno:64040.
    UCSCi RGD:68409. rat.

    Organism-specific databases

    CTDi 223.
    RGDi 68409. Aldh9a1.

    Phylogenomic databases

    eggNOGi COG1012.
    GeneTreei ENSGT00720000108597.
    HOGENOMi HOG000271505.
    HOVERGENi HBG000097.
    InParanoidi Q9JLJ3.
    KOi K00149.
    OrthoDBi EOG7327P4.
    PhylomeDBi Q9JLJ3.

    Enzyme and pathway databases

    UniPathwayi UPA00118 .
    BioCyci MetaCyc:MONOMER-14430.
    SABIO-RK Q9JLJ3.

    Miscellaneous databases

    NextBioi 612685.
    PROi Q9JLJ3.

    Gene expression databases

    Genevestigatori Q9JLJ3.

    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], PARTIAL PROTEIN SEQUENCE, FUNCTION, CHARACTERIZATION.
      Strain: Wistar.
      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].
      Tissue: Heart.
    3. Lubec G., Afjehi-Sadat L., Kang S.U.
      Submitted (JUL-2007) to UniProtKB
      Cited for: PROTEIN SEQUENCE OF 50-59; 199-223; 275-293 AND 412-426, IDENTIFICATION BY MASS SPECTROMETRY.
      Strain: Sprague-Dawley.
      Tissue: Brain and Spinal cord.

    Entry informationi

    Entry nameiAL9A1_RAT
    AccessioniPrimary (citable) accession number: Q9JLJ3
    Secondary accession number(s): Q6GMM4
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 1, 2005
    Last sequence update: October 1, 2000
    Last modified: October 1, 2014
    This is version 98 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. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3