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Q9JLJ3 (AL9A1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 97. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus

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. Ref.1

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.

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_0000056489

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 By similarity
Modified residue301N6-succinyllysine; alternate By similarity
Modified residue591N6-succinyllysine By similarity
Modified residue2981N6-acetyllysine By similarity

Experimental info

Sequence conflict493 – 4942AF → PFENQ in AAH74019. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q9JLJ3 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: E417BD52D7DF567C

FASTA49453,653
        10         20         30         40         50         60 
MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGREI ATFKCSGEKE VNLAVENAKA 

        70         80         90        100        110        120 
AFKIWSKKSG LERCQVLLEA ARIIKERRDE IAIMETINNG KSIFEARLDV DTSWQCLEYY 

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

       190        200        210        220        230        240 
PSPFTPVSAL LLAEIYTKAG APNGLFNVVQ GGAATGQFLC QHRDVAKVSF TGSVPTGMKI 

       250        260        270        280        290        300 
MEMAAKGIKP ITLELGGKSP LIIFSDCNMK NAVKGALLAN FLTQGQVCCN GTRVFVQKEI 

       310        320        330        340        350        360 
ADAFTKEVVR QTQRIKIGDP LLEDTRMGPL INAPHLERVL GFVRSAKEQG ATVLCGGEPY 

       370        380        390        400        410        420 
APEDPKLKHG YYMTPCILTN CTDDMTCVKE EIFGPVMSIL TFETEAEVLE 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], 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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF170918 mRNA. Translation: AAF43598.1.
BC074019 mRNA. Translation: AAH74019.1.
RefSeqNP_071609.2. NM_022273.2.
UniGeneRn.98155.

3D structure databases

ProteinModelPortalQ9JLJ3.
SMRQ9JLJ3. Positions 2-492.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActQ9JLJ3. 1 interaction.
MINTMINT-4580055.

PTM databases

PhosphoSiteQ9JLJ3.

Proteomic databases

PaxDbQ9JLJ3.
PRIDEQ9JLJ3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSRNOT00000005611; ENSRNOP00000005611; ENSRNOG00000004027.
GeneID64040.
KEGGrno:64040.
UCSCRGD:68409. rat.

Organism-specific databases

CTD223.
RGD68409. Aldh9a1.

Phylogenomic databases

eggNOGCOG1012.
GeneTreeENSGT00720000108597.
HOGENOMHOG000271505.
HOVERGENHBG000097.
InParanoidQ9JLJ3.
KOK00149.
OrthoDBEOG7327P4.
PhylomeDBQ9JLJ3.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-14430.
SABIO-RKQ9JLJ3.
UniPathwayUPA00118.

Gene expression databases

GenevestigatorQ9JLJ3.

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_CYS.
IPR029510. Ald_DH_CS_GLU.
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

NextBio612685.
PROQ9JLJ3.

Entry information

Entry nameAL9A1_RAT
AccessionPrimary (citable) accession number: Q9JLJ3
Secondary accession number(s): Q6GMM4
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 2005
Last sequence update: October 1, 2000
Last modified: June 11, 2014
This is version 97 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