4-trimethylaminobutyraldehyde dehydrogenase

Contribute

Send feedback

Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot Q9JLJ3 (AL9A1_RAT)

Last modified January 19, 2010. Version 62. History...

Clusters with 100%, 90%, 50% identity |

Documents (2) |

Third-party data |

Customize display

text xml rdf/xml gff fasta

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Hide | Top

Names and origin

Protein names

Recommended 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

Organism

Rattus norvegicus (Rat)

Taxonomic identifier

10116 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Hide | Top

Protein attributes

Sequence length	494 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

Hide | Top

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 = an acid + NADH.
Pathway	Amine and polyamine biosynthesis; carnitine biosynthesis.
Subunit structure	Homotetramer By similarity.
Subcellular location	Cytoplasm.
Sequence similarities	Belongs to the aldehyde dehydrogenase family.

Hide | Top

Ontologies

Keywords
Cellular component	Cytoplasm
Ligand	NAD
Molecular function	Oxidoreductase
PTM	Acetylation
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	carnitine biosynthetic process Ref.1 Traceable author statement. Source: RGD kidney development Inferred from expression pattern. Source: RGD liver development Inferred from expression pattern. Source: RGD oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.1 Inferred from direct assay. Source: RGD
Molecular function	4-trimethylammoniobutyraldehyde dehydrogenase activity Ref.1 Inferred from direct assay. Source: RGD NAD or NADH binding Inferred from direct assay. Source: RGD aldehyde dehydrogenase (NAD) activity Ref.1 Inferred from direct assay. Source: RGD amine binding Inferred from direct assay. Source: RGD aminobutyraldehyde dehydrogenase activity Ref.1 Inferred from direct assay. Source: RGD protein homodimerization activity Inferred from direct assay. Source: RGD
Complete GO annotation...

Hide | Top

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed By similarity

Chain

2 – 494

493

4-trimethylaminobutyraldehyde dehydrogenase

PRO_0000056489

Regions

Nucleotide binding

232 – 237

NAD By similarity

Sites

Active site

254

Potential

Active site

288

Potential

Amino acid modifications

Modified residue

N-acetylserine By similarity

Modified residue

298

N6-acetyllysine By similarity

Experimental info

Sequence conflict

493 – 494

AF → PFENQ in AAH74019. Ref.2

Hide | Top

Sequences

Sequence

Length

Mass (Da)

Tools

Q9JLJ3-1 [UniParc].

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

FASTA

494

53,653

        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

Hide | Top

References

	« Hide 'large scale' referencesShow '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: 10702312] [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: 15489334] [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, MASS SPECTROMETRY. Strain: Sprague-Dawley. Tissue: Brain and Spinal cord.
+	Additional computationally mapped references.

Hide | Top

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF170918 mRNA. Translation: AAF43598.1. BC074019 mRNA. Translation: AAH74019.1.
IPI	IPI00203690.
RefSeq	NP_071609.2.
UniGene	Rn.98155
3D structure databases
SMR	Q9JLJ3. Positions 2-492.
ModBase	Search...
Protein-protein interaction databases
STRING	Q9JLJ3.
Proteomic databases
PRIDE	Q9JLJ3.
Genome annotation databases
Ensembl	ENSRNOT00000005611; ENSRNOP00000005611; ENSRNOG00000004027; Rattus norvegicus. [Genome view]
GeneID	64040.
KEGG	rno:64040.
UCSC	NM_022273. rat.
Organism-specific databases
CTD	64040.
RGD	68409. Aldh9a1.
Phylogenomic databases
eggNOG	roNOG12605.
HOVERGEN	Q9JLJ3.
InParanoid	Q9JLJ3.
PhylomeDB	Q9JLJ3.
Enzyme and pathway databases
BioCyc	MetaCyc:MONOMER-14430.
BRENDA	1.2.1.3. 248. 1.2.1.47. 248.
Gene expression databases
ArrayExpress	Q9JLJ3.
Genevestigator	Q9JLJ3.
GermOnline	ENSRNOG00000004027. Rattus norvegicus.
Family and domain databases
InterPro	IPR016161. Ald_DH/histidinol_DH. IPR016160. Ald_DH_CS. IPR016162. Ald_DH_N. IPR015590. Aldehyde_DH. [Graphical view]
Gene3D	G3DSA:3.40.605.10. Aldehyde_dehydrogenase_N. 1 hit.
PANTHER	PTHR11699. Aldehyde_dehyd. 1 hit.
Pfam	PF00171. Aldedh. 1 hit. [Graphical view]
PROSITE	PS00070. ALDEHYDE_DEHYDR_CYS. 1 hit. PS00687. ALDEHYDE_DEHYDR_GLU. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	612685.

Hide | Top

Entry information

Entry name

AL9A1_RAT

Accession

Primary (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:	January 19, 2010
This is version 62 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

Hide | Top

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Regions

Sites

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents