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Protein

4-trimethylaminobutyraldehyde dehydrogenase

Gene

Aldh9a1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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.

Pathway:icarnitine biosynthesis

This protein is involved in the pathway carnitine biosynthesis, which is part of Amine and polyamine biosynthesis.
View all proteins of this organism that are known to be involved in the pathway carnitine biosynthesis and in Amine and polyamine biosynthesis.

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

  • 4-trimethylammoniobutyraldehyde dehydrogenase activity Source: RGD
  • aldehyde dehydrogenase (NAD) activity Source: RGD
  • amine binding Source: RGD
  • aminobutyraldehyde dehydrogenase activity Source: RGD
  • NAD binding Source: RGD
  • protein homodimerization activity Source: RGD

GO - Biological processi

  • carnitine biosynthetic process Source: RGD
  • kidney development Source: RGD
  • liver development Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Oxidoreductase

Keywords - Ligandi

NAD

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-14430.
BRENDAi1.2.1.47. 5301.
ReactomeiREACT_345009. Carnitine synthesis.
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 Componenti: Unplaced

Organism-specific databases

RGDi68409. Aldh9a1.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: RGD
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_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

GenevisibleiQ9JLJ3. RN.

Interactioni

Subunit structurei

Homotetramer.By similarity

Protein-protein interaction databases

IntActiQ9JLJ3. 1 interaction.
MINTiMINT-4580055.
STRINGi10116.ENSRNOP00000005611.

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.
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

        10         20         30         40         50
MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGREI ATFKCSGEKE
60 70 80 90 100
VNLAVENAKA AFKIWSKKSG LERCQVLLEA ARIIKERRDE IAIMETINNG
110 120 130 140 150
KSIFEARLDV DTSWQCLEYY AGLAASMAGE HIQLPGGSFG YTRREPLGVC
160 170 180 190 200
LGIGAWNYPF QIACWKSAPA LACGNAMIFK PSPFTPVSAL LLAEIYTKAG
210 220 230 240 250
APNGLFNVVQ GGAATGQFLC QHRDVAKVSF TGSVPTGMKI MEMAAKGIKP
260 270 280 290 300
ITLELGGKSP LIIFSDCNMK NAVKGALLAN FLTQGQVCCN GTRVFVQKEI
310 320 330 340 350
ADAFTKEVVR QTQRIKIGDP LLEDTRMGPL INAPHLERVL GFVRSAKEQG
360 370 380 390 400
ATVLCGGEPY APEDPKLKHG YYMTPCILTN CTDDMTCVKE EIFGPVMSIL
410 420 430 440 450
TFETEAEVLE RANDTTFGLA AGVFTRDIQR AHRVAAELQA GTCYINNYNV
460 470 480 490
SPVELPFGGY KKSGFGRENG RVTIEYYSQL KTVCVEMGDV ESAF
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:
EMBLi
GenBanki
DDBJi
Links Updated
AF170918 mRNA. Translation: AAF43598.1.
BC074019 mRNA. Translation: AAH74019.1.
RefSeqiNP_071609.2. NM_022273.2.
UniGeneiRn.98155.

Genome annotation databases

GeneIDi64040.
KEGGirno:64040.
UCSCiRGD:68409. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF170918 mRNA. Translation: AAF43598.1.
BC074019 mRNA. Translation: AAH74019.1.
RefSeqiNP_071609.2. NM_022273.2.
UniGeneiRn.98155.

3D structure databases

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

Protein-protein interaction databases

IntActiQ9JLJ3. 1 interaction.
MINTiMINT-4580055.
STRINGi10116.ENSRNOP00000005611.

PTM databases

PhosphoSiteiQ9JLJ3.

Proteomic databases

PaxDbiQ9JLJ3.
PRIDEiQ9JLJ3.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi64040.
KEGGirno:64040.
UCSCiRGD:68409. rat.

Organism-specific databases

CTDi223.
RGDi68409. Aldh9a1.

Phylogenomic databases

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

Enzyme and pathway databases

UniPathwayiUPA00118.
BioCyciMetaCyc:MONOMER-14430.
BRENDAi1.2.1.47. 5301.
ReactomeiREACT_345009. Carnitine synthesis.
SABIO-RKQ9JLJ3.

Miscellaneous databases

NextBioi612685.
PROiQ9JLJ3.

Gene expression databases

GenevisibleiQ9JLJ3. RN.

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], 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: July 22, 2015
This is version 106 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

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.