[1]	NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE, FUNCTION, AND CHARACTERIZATION. STRAIN=Wistar; TISSUE=Liver; DOI=10.1074/jbc.275.10.7390; PubMed=10702312 [NCBI, ExPASy, EBI, Israel, Japan] Vaz F.M., Fouchier S.W., Ofman R., Sommer M., Wanders R.J.A.; "Molecular and biochemical characterization of rat gamma-trimethylaminobutyraldehyde dehydrogenase and evidence for the involvement of human aldehyde dehydrogenase 9 in carnitine biosynthesis."; J. Biol. Chem. 275:7390-7394(2000).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. TISSUE=Heart; DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan] The MGC Project Team; "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."; Genome Res. 14:2121-2127(2004).
[3]	PROTEIN SEQUENCE OF 50-59; 199-223; 275-293 AND 412-426, AND MASS SPECTROMETRY. STRAIN=Sprague-Dawley; TISSUE=Brain, and Spinal cord; Lubec G., Afjehi-Sadat L., Kang S.U.; Submitted (JUL-2007) to UniProtKB.

Comments

FUNCTION: Converts gamma-trimethylaminobutyraldehyde into gamma-butyrobetaine.
CATALYTIC ACTIVITY: 4-trimethylammoniobutanal + NAD⁺ + H₂O = 4-trimethylammoniobutanoate + NADH.
CATALYTIC ACTIVITY: An aldehyde + NAD⁺ + H₂O = an acid + NADH.
PATHWAY: Amine and polyamine biosynthesis; carnitine biosynthesis .
SUBUNIT: Homotetramer (By similarity).
SUBCELLULAR LOCATION: Cytoplasm.
SIMILARITY: Belongs to the aldehyde dehydrogenase family.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

AF170918; AAF43598.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BC074019; AAH74019.1; -; mRNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_071609.2; -.

UniGene

Rn.98155

3D structure databases

HSSP

P56533; 1A4S. [HSSP ENTRY / PDB]

ModBase

Q9JLJ3.

Organism-specific databases

RGD

68409; Aldh9a1.

Gene expression databases

ArrayExpress

Q9JLJ3; -.

GermOnline

ENSRNOG00000004027; Rattus norvegicus.

Ontologies

GO:0047105;	Molecular function: 4-trimethylammoniobutyraldehyde dehydrogenase activity (inferred from electronic annotation from EC).
GO:0004029;	Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from electronic annotation from EC).
GO:0055114;	Biological process: oxidation reduction (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.

Family and domain databases

InterPro

IPR016160; Ald_DHase_CS.
IPR016162; Ald_DHase_N.
IPR015590; Aldehyde_DHase.
Graphical view of domain structure.

Gene3D

G3DSA:3.40.605.10; Aldehyde_dehydrogenase_N; 1.

PANTHER

PTHR11699; Aldehyde_dehyd; 1.

Pfam

PF00171; Aldedh; 1.
Pfam graphical view of domain structure.

PROSITE

PS00070; ALDEHYDE_DEHYDR_CYS; 1.
PS00687; ALDEHYDE_DEHYDR_GLU; 1.

Genome annotation databases

Ensembl

ENSRNOG00000004027; Rattus norvegicus. [Contig view]

GeneID

64040; -.

KEGG

rno:64040; -.

Phylogenomic databases

HOVERGEN

Q9JLJ3; -.

Other

NextBio

612685; -.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`INIT_MET`	`1 1`		`Removed (By similarity).`
`CHAIN`	`2 494`	`493`	`4-trimethylaminobutyraldehyde dehydrogenase.`	`PRO_0000056489`
`NP_BIND`	`232 237`	`6`	`NAD (By similarity).`
`ACT_SITE`	`254 254`		`Potential.`
`ACT_SITE`	`288 288`		`Potential.`
`MOD_RES`	`2 2`		`N-acetylserine (By similarity).`
`CONFLICT`	`493 494`		`AF -> PFENQ (in Ref. 2; AAH74019).`

Sequence information

Length: 494 AA [This is the length of the unprocessed precursor]

Molecular weight: 53653 Da [This is the MW of the unprocessed precursor]

CRC64: E417BD52D7DF567C [This is a checksum on the sequence]

        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

Q9JLJ3 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools