Sequence of AL9A1_MOUSE
EC Number:1.2.1.3
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
an aldehyde + NAD+ + H2O = a carboxylate + NADH + H+
Other sequences found for EC No. 1.2.1.3
EC Number:1.2.1.47
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
4-trimethylammoniobutanal + NAD+ + H2O = 4-trimethylammoniobutanoate + NADH + 2 H+
Other sequences found for EC No. 1.2.1.47
General information:
Sequence
0 MSTGTFVVSQ PLNYRGGARV EPVDASGTEK AFEPATGRVI ATFACSGEKE VNLAVENAKA
60 AFKLWSKKSG LERCQVLLEA ARIIKERKDE IATVETINNG KSIFEARLDV DTCWQCLEYY
120 AGLAASMAGE HIQLPGGSFG YTRREPLGVC VGIGAWNYPF QIACWKSAPA LACGNAMIFK
180 PSPFTPVSAL LLAEIYTKAG APPGLFNVVQ GGAATGQFLC HHREVAKISF TGSVPTGVKI
240 MEMSAKGVKP ITLELGGKSP LIIFSDCNME NAVKGALMAN FLTQGQVCCN GTRVFVQKEI
300 ADKFINEVVK QTQKIKLGDP LLEDTRMGPL INAPHLERVL GFVKLAKEQG ATVLCGGEVY
360 VPEDPKLKHG YYMTPCILTN CRDDMTCVKE EIFGPVMSIL TFGTEAEVLE RANDTTFGLA
420 AGVFTRDIQR AHRVAAELQA GTCYINNYNV SPVELPFGGY KKSGFGRENG RVTIEYYSQL
480 KTVCVEMGDV ESAF
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
767099
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
767100
Okazaki Y.,Furuno M.,Kasukawa T.,Adachi J.,Bono H.,Kondo S.,Nikaido I.,Osato N.,Saito R.,Suzuki H.,Yamanaka I.,Kiyosawa H.,Yagi K.,Tomaru Y.,Hasegawa Y.,Nogami A.,Schonbach C.,Gojobori T.,Baldarelli R.,Hill D.P.,Bult C.,Hume D.A.,Quackenbush J.,Schriml L.M.,Kanapin A.,Matsuda H.,Batalov S.,Beisel K.W.,Blake J.A.,Bradt D.,Brusic V.,Chothia C.,Corbani L.E.,Cousins S.,Dalla E.,Dragani T.A.,Fletcher C.F.,Forrest A.,Frazer K.S.,Gaasterland T.,Gariboldi M.,Gissi C.,Godzik A.,Gough J.,Grimmond S.,Gustincich S.,Hirokawa N.,Jackson I.J.,Jarvis E.D.,Kanai A.,Kawaji H.,Kawasawa Y.,Kedzierski R.M.,King B.L.,Konagaya A.,Kurochkin I.V.,Lee Y.,Lenhard B.,Lyons P.A.,Maglott D.R.,Maltais L.,Marchionni L.,McKenzie L.,Miki H.,Nagashima T.,Numata K.,Okido T.,Pavan W.J.,Pertea G.,Pesole G.,Petrovsky N.,Pillai R.,Pontius J.U.,Qi D.,Ramachandran S.,Ravasi T.,Reed J.C.,Reed D.J.,Reid J.,Ring B.Z.,Ringwald M.,Sandelin A.,Schneider C.,Semple C.A.,Setou M.,Shimada K.,Sultana R.,Takenaka Y.,Taylor M.S.,Teasdale R.D.,Tomita M.,Verardo R.,Wagner L.,Wahlestedt C.,Wang Y.,Watanabe Y.,Wells C.,Wilming L.G.,Wynshaw-Boris A.,Yanagisawa M.,Yang I.,Yang L.,Yuan Z.,Zavolan M.,Zhu Y.,Zimmer A.,Carninci P.,Hayatsu N.,Hirozane-Kishikawa T.,Konno H.,Nakamura M.,Sakazume N.,Sato K.,Shiraki T.,Waki K.,Kawai J.,Aizawa K.,Arakawa T.,Fukuda S.,Hara A.,Hashizume W.,Imotani K.,Ishii Y.,Itoh M.,Kagawa I.,Miyazaki A.,Sakai K.,Sasaki D.,Shibata K.,Shinagawa A.,Yasunishi A.,Yoshino M.,Waterston R.,Lander E.S.,Rogers J.,Birney E.,Hayashizaki Y.
Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Nature
420
563-573
2002
767101
Church D.M.,Goodstadt L.,Hillier L.W.,Zody M.C.,Goldstein S.,She X.,Bult C.J.,Agarwala R.,Cherry J.L.,DiCuccio M.,Hlavina W.,Kapustin Y.,Meric P.,Maglott D.,Birtle Z.,Marques A.C.,Graves T.,Zhou S.,Teague B.,Potamousis K.,Churas C.,Place M.,Herschleb J.,Runnheim R.,Forrest D.,Amos-Landgraf J.,Schwartz D.C.,Cheng Z.,Lindblad-Toh K.,Eichler E.E.,Ponting C.P.
Lineage-specific biology revealed by a finished genome assembly of the mouse.
PLoS Biol.
7
0-0
2009
767102
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
767104
Huttlin E.L.,Jedrychowski M.P.,Elias J.E.,Goswami T.,Rad R.,Beausoleil S.A.,Villen J.,Haas W.,Sowa M.E.,Gygi S.P.
A tissue-specific atlas of mouse protein phosphorylation and expression.
Cell
143
1174-1189
2010
767105
Park J.,Chen Y.,Tishkoff D.X.,Peng C.,Tan M.,Dai L.,Xie Z.,Zhang Y.,Zwaans B.M.,Skinner M.E.,Lombard D.B.,Zhao Y.
SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways.
Mol. Cell
50
919-930
2013
767106
Rardin M.J.,Newman J.C.,Held J.M.,Cusack M.P.,Sorensen D.J.,Li B.,Schilling B.,Mooney S.D.,Kahn C.R.,Verdin E.,Gibson B.W.
Label-free quantitative proteomics of the lysine acetylome in mitochondria identifies substrates of SIRT3 in metabolic pathways.
Proc. Natl. Acad. Sci. U.S.A.
110
6601-6606
2013
