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UniProtKB/Swiss-Prot entry P49189


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AL9A1_HUMAN
Primary accession number P49189
Secondary accession numbers Q5VV90 Q6LCL1 Q9NZT7
Integrated into Swiss-Prot on February 1, 1996
Sequence was last modified on February 1, 2005 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 77)
Name and origin of the protein
Protein name 4-trimethylaminobutyraldehyde dehydrogenase
Synonyms TMABADH
EC 1.2.1.47
Aldehyde dehydrogenase family 9 member A1
EC 1.2.1.3
Aldehyde dehydrogenase E3 isozyme
Gamma-aminobutyraldehyde dehydrogenase
EC 1.2.1.19
R-aminobutyraldehyde dehydrogenase
Gene name
Name: ALDH9A1
Synonyms: ALDH4, ALDH7, ALDH9
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-116.
TISSUE=Liver;
DOI=10.1006/geno.1996.0300; PubMed=8786138 [NCBI, ExPASy, EBI, Israel, Japan]
Lin S.W., Chen J.C., Hsu L.C., Hsieh C.-L., Yoshida A.;
"Human gamma-aminobutyraldehyde dehydrogenase (ALDH9): cDNA sequence, genomic organization, polymorphism, chromosomal localization, and tissue expression.";
Genomics 34:376-380(1996).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND FUNCTION.
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
PROTEIN SEQUENCE OF 2-15; 247-258; 299-310; 315-326 AND 472-481, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
TISSUE=Colon carcinoma;
Bienvenut W.V., Heiserich L., Gottlieb E.;
Submitted (MAR-2008) to UniProtKB.
[5]
PROTEIN SEQUENCE OF 259-274; 353-366; 412-426 AND 434-453, NUCLEOTIDE SEQUENCE [MRNA] OF 29-494, CHARACTERIZATION, TISSUE SPECIFICITY, AND VARIANT SER-116.
TISSUE=Brain;
PubMed=8645224 [NCBI, ExPASy, EBI, Israel, Japan]
Kikonyogo A., Pietruszko R.;
"Aldehyde dehydrogenase from adult human brain that dehydrogenates gamma-aminobutyraldehyde: purification, characterization, cloning and distribution.";
Biochem. J. 316:317-324(1996).
[6]
NUCLEOTIDE SEQUENCE [MRNA] OF 33-494, AND PARTIAL PROTEIN SEQUENCE.
PubMed=8269919 [NCBI, ExPASy, EBI, Israel, Japan]
Kurys G., Shah P.C., Kikonyogo A., Reed D., Ambroziak W., Pietruszko R.;
"Human aldehyde dehydrogenase. cDNA cloning and primary structure of the enzyme that catalyzes dehydrogenation of 4-aminobutyraldehyde.";
Eur. J. Biochem. 218:311-320(1993).
[7]
CHARACTERIZATION.
TISSUE=Liver;
PubMed=2925663 [NCBI, ExPASy, EBI, Israel, Japan]
Kurys G., Ambroziak W., Pietruszko R.;
"Human aldehyde dehydrogenase. Purification and characterization of a third isozyme with low Km for gamma-aminobutyraldehyde.";
J. Biol. Chem. 264:4715-4721(1989).
Comments
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
U34252; AAB18827.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF172093; AAF43600.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL451074; CAH74061.1; ALT_INIT; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U50203; AAB06721.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X75425; CAA53176.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR G02054; S39532.
RefSeq NP_000687.3; -.
UniGene Hs.2533
3D structure databases
HSSP P56533; 1A4S. [HSSP ENTRY / PDB]
SMR P49189; 2-494.
ModBase P49189.
PTM databases
PhosphoSite P49189; -.
2D gel databases
REPRODUCTION-2DPAGE IPI00479877; -.
Organism-specific databases
H-InvDB HIX0001281; -.
HGNC HGNC:412; ALDH9A1.
GenAtlas ALDH9A1.
HPA HPA006077; -.
HPA010873; -.
MIM 602733; gene. [NCBI / EBI]
PharmGKB PA24706; -.
GeneCards P49189.
Gene expression databases
CleanEx HS_ALDH9A1; -.
GermOnline ENSG00000143149; Homo sapiens.
Ontologies
GO
GO:0005737; Cellular component: cytoplasm (traceable author statement from UniProtKB).
GO:0004029; Molecular function: aldehyde dehydrogenase (NAD) activity (inferred from direct assay from UniProtKB).
GO:0019145; Molecular function: aminobutyraldehyde dehydrogenase activity (inferred from direct assay from UniProtKB).
GO:0006081; Biological process: cellular aldehyde metabolic process (inferred from direct assay from UniProtKB).
GO:0042445; Biological process: hormone metabolic process (traceable author statement from UniProtKB).
GO:0042136; Biological process: neurotransmitter biosynthetic process (inferred from direct assay from UniProtKB).
GO:0055114; Biological process: oxidation reduction (inferred from direct assay from UniProtKB).
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.
BLOCKS P49189.
Genome annotation databases
Ensembl ENSG00000143149; Homo sapiens. [Contig view]
GeneID 223; -.
KEGG hsa:223; -.
Phylogenomic databases
HOGENOM P49189; -.
HOVERGEN P49189; -.
Other
DrugBank DB00157; NADH.
SOURCE ALDH9A1; Homo sapiens.
ProtoNet P49189.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Cytoplasm; Direct protein sequencing; NAD; Oxidoreductase; Polymorphism.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   494  493     4-trimethylaminobutyraldehyde dehydrogenase. PRO_0000056485
NP_BIND   232   237  6     NAD (By similarity). 
ACT_SITE   254   254        Proton acceptor (By similarity). 
ACT_SITE   288   288        Nucleophile (By similarity). 
SITE   157   157  1     Transition state stabilizer (By similarity). 
MOD_RES   2     2        N-acetylserine. 
VARIANT   116   116  1     C -> S (in allele ALDH9A1*2). VAR_011304 [3D]
CONFLICT   19    25        RVEPADA -> AGAGGR (in Ref. 1; AAB18827). 
CONFLICT   150   150        C -> Q (in Ref. 6; AA sequence). 
CONFLICT   159   159        P -> W (in Ref. 6; AA sequence). 
CONFLICT   172   172        A -> R (in Ref. 6; AA sequence). 
Sequence information
Length: 494 AA [This is the length of the unprocessed precursor] Molecular weight: 53802 Da [This is the MW of the unprocessed precursor] CRC64: 1E1CDF910D763BA1 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSTGTFVVSQ PLNYRGGARV EPADASGTEK AFEPATGRVI ATFTCSGEKE VNLAVQNAKA 

        70         80         90        100        110        120 
AFKIWSQKSG MERCRILLEA ARIIREREDE IATMECINNG KSIFEARLDI DISWQCLEYY 

       130        140        150        160        170        180 
AGLAASMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QIASWKSAPA LACGNAMVFK 

       190        200        210        220        230        240 
PSPFTPVSAL LLAEIYSEAG VPPGLFNVVQ GGAATGQFLC QHPDVAKVSF TGSVPTGMKI 

       250        260        270        280        290        300 
MEMSAKGIKP VTLELGGKSP LIIFSDCDMN NAVKGALMAN FLTQGQVCCN GTRVFVQKEI 

       310        320        330        340        350        360 
LDKFTEEVVK QTQRIKIGDP LLEDTRMGPL INRPHLERVL GFVKVAKEQG AKVLCGGDIY 

       370        380        390        400        410        420 
VPEDPKLKDG YYMRPCVLTN CRDDMTCVKE EIFGPVMSIL SFDTEAEVLE RANDTTFGLA 

       430        440        450        460        470        480 
AGVFTRDIQR AHRVVAELQA GTCFINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL 

       490 
KTVCVEMGDV ESAF 

P49189 in FASTA format

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View entry in raw text format (no links)
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