Sequence of AL1L1_RAT
EC Number:1.5.1.6
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
10-formyltetrahydrofolate + NADP+ + H2O = tetrahydrofolate + CO2 + NADPH + H+
Other sequences found for EC No. 1.5.1.6
General information:
Sequence
0 MKIAVIGQSL FGQEVYCQLR KEGHEVVGVF TIPDKDGKAD PLGLEAEKDG VPVFKFPRWR
60 ARGQALPEVV AKYQALGAEL NVLPFCSQFI PMEVINAPRH GSIIYHPSLL PRHRGASAIN
120 WTLIHGDKKG GFTIFWADDG LDTGDLLLQK ECEVLPDDTV STLYNRFLFP EGIKGMVQAV
180 RLIAEGTAPR CPQSEEGATY EGIQKKETAK INWDQPAEAI HNWIRGNDKV PGAWTEACGQ
240 KLTFFNSTLN TSGLSTQGEA LPIPGAHRPG VVTKAGLILF GNDDRMLLVK NIQLEDGKMM
300 PASQFFKGSA SSDLELTEAE LATAEAVRSS WMRILPNVPE VEDSTDFFKS GAASVDVVRL
360 VEEVKELCDG LELENEDVYM ATTFRGFIQL LVRKLRGEDD ESECVINYVE KAVNKLTLQM
420 PYQLFIGGEF VDAEGSKTYN TINPTDGSVI CQVSLAQVSD VDKAVAAAKE AFENGLWGKI
480 NARDRGRLLY RLADVMEQHQ EELATIEALD AGAVYTLALK THVGMSIQTF RYFAGWCDKI
540 QGATIPINQA RPNRNLTLTK KEPVGVCGIV IPWNYPLMML SWKTAACLAA GNTVVIKPAQ
600 VTPLTALKFA ELTLKAGIPK GVVNILPGSG SLVGQRLSDH PDVRKIGFTG STEVGKHIMK
660 SCALSNVKKV SLELGGKSPL IIFADCDLNK AVQMGMSSVF FNKGENCIAA GRLFVEESIH
720 NQFVQKVVEE VEKMKIGNPL ERDTNHGPQN HEAHLRKLVE YCQRGVKEGA TLVCGGNQVP
780 RPGFFFQPTV FTDVEDHMYI AKEESFGPIM IISRFADGDV DAVLSRANAT EFGLASGVFT
840 RDINKALYVS DKLQAGTVFI NTYNKTDVAA PFGGFKQSGF GKDLGEAALN EYLRIKTVTF
900 EY
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
130353
Cook R.J.,Lloyd R.S.,Wagner C.
Isolation and characterization of cDNA clones for rat liver 10-formyltetrahydrofolate dehydrogenase.
J. Biol. Chem.
266
4965-4973
1991
130354
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).
Genome Res.
14
2121-2127
2004
130355
Krupenko S.A.,Wagner C.
Aspartate 142 is involved in both hydrolase and dehydrogenase catalytic centers of 10-formyltetrahydrofolate dehydrogenase.
J. Biol. Chem.
274
35777-35784
1999
130356
Case G.L.,Kaisaki P.J.,Steele R.D.
Resolution of rat liver 10-formyltetrahydrofolate dehydrogenase/hydrolase activities.
J. Biol. Chem.
263
10204-10207
1988
130357
Krupenko S.A.,Wagner C.,Cook R.J.
Cysteine 707 is involved in the dehydrogenase activity site of rat 10-formyltetrahydrofolate dehydrogenase.
J. Biol. Chem.
270
519-522
1995
130358
Moser K.,White F.M.
Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-MS/MS.
J. Proteome Res.
5
98-104
2006
130359
Donato H.,Krupenko N.I.,Tsybovsky Y.,Krupenko S.A.
10-formyltetrahydrofolate dehydrogenase requires a 4'-phosphopantetheine prosthetic group for catalysis.
J. Biol. Chem.
282
34159-34166
2007
130360
Lundby A.,Secher A.,Lage K.,Nordsborg N.B.,Dmytriyev A.,Lundby C.,Olsen J.V.
Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues.
Nat. Commun.
3
876-876
2012
130361
Chumanevich A.A.,Krupenko S.A.,Davies C.
The crystal structure of the hydrolase domain of 10-formyltetrahydrofolate dehydrogenase: mechanism of hydrolysis and its interplay with the dehydrogenase domain.
J. Biol. Chem.
279
14355-14364
2004
130362
Tsybovsky Y.,Donato H.,Krupenko N.I.,Davies C.,Krupenko S.A.
Crystal structures of the carboxyl terminal domain of rat 10-formyltetrahydrofolate dehydrogenase: implications for the catalytic mechanism of aldehyde dehydrogenases.
Biochemistry
46
2917-2929
2007
130363
Tsybovsky Y.,Krupenko S.A.
Conserved catalytic residues of the ALDH1L1 aldehyde dehydrogenase domain control binding and discharging of the coenzyme.
J. Biol. Chem.
286
23357-23367
2011
