Reviewed, UniProtKB/Swiss-Prot Q9JLJ3 (AL9A1_RAT)

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

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.

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.

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 oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytosol Ref.1 Non-traceable author statement. Source: RGD
Molecular function	4-trimethylammoniobutyraldehyde dehydrogenase activity Inferred from electronic annotation. Source: EC aldehyde dehydrogenase (NAD) activity Ref.1 Inferred from direct assay. Source: RGD
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 494	493	4-trimethylaminobutyraldehyde dehydrogenase		PRO_0000056489
Regions
	Nucleotide binding	232 – 237	6	NAD By similarity
Sites
	Active site	254	1	Potential
	Active site	288	1	Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
Experimental info
	Sequence conflict	493 – 494	2	AF → PFENQ in AAH74019. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9JLJ3-1 [UniParc]. Last modified October 1, 2000. Version 1. Checksum: E417BD52D7DF567C	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

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.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF170918 mRNA. Translation: AAF43598.1. BC074019 mRNA. Translation: AAH74019.1.
IPI	IPI00203690.
RefSeq	NP_071609.2.
UniGene	Rn.98155
3D structure databases
HSSP	HSSP built from PDB template 1A4S based on UniProtKB P56533.
ModBase	Search...
Proteomic databases
PRIDE	Q9JLJ3.
Genome annotation databases
Ensembl	ENSRNOG00000004027. Rattus norvegicus. [Contig view]
GeneID	64040.
KEGG	rno:64040.
Organism-specific databases
RGD	68409. Aldh9a1.
Phylogenomic databases
HOVERGEN	Q9JLJ3.
Enzyme and pathway databases
BRENDA	1.2.1.3. 248. 1.2.1.47. 248.
Gene expression databases
ArrayExpress	Q9JLJ3.
GermOnline	ENSRNOG00000004027. Rattus norvegicus.
Family and domain databases
InterPro	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.

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:	June 16, 2009
This is version 56 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)