Sequence of HICDH_THET2
EC Number:1.1.1.286
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
isocitrate-homoisocitrate dehydrogenase
Q72IW9
Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)
334
35922
Reaction
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + NAD+ = 2-oxoadipate + CO2 + NADH + H+
Other sequences found for EC No. 1.1.1.286
General information:
Sequence
0 MAYRICLIEG DGIGHEVIPA ARRVLEATGL PLEFVEAEAG WETFERRGTS VPEETVEKIL
60 SCHATLFGAA TSPTRKVPGF FGAIRYLRRR LDLYANVRPA KSRPVPGSRP GVDLVIVREN
120 TEGLYVEQER RYLDVAIADA VISKKASERI GRAALRIAEG RPRKTLHIAH KANVLPLTQG
180 LFLDTVKEVA KDFPLVNVQD IIVDNCAMQL VMRPERFDVI VTTNLLGDIL SDLAAGLVGG
240 LGLAPSGNIG DTTAVFEPVH GSAPDIAGKG IANPTAAILS AAMMLDYLGE KEAAKRVEKA
300 VDLVLERGPR TPDLGGDATT EAFTEAVVEA LKSL
Download this sequence
in fasta formatDownload all sequences for 1.1.1.286
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
302240
Miyazaki J.,Kobashi N.,Nishiyama M.,Yamane H.
Characterization of homoisocitrate dehydrogenase involved in lysine biosynthesis of an extremely thermophilic bacterium, Thermus thermophilus HB27, and evolutionary implication of beta-decarboxylating dehydrogenase.
J. Biol. Chem.
278
1864-1871
2003
302241
Henne A.,Brueggemann H.,Raasch C.,Wiezer A.,Hartsch T.,Liesegang H.,Johann A.,Lienard T.,Gohl O.,Martinez-Arias R.,Jacobi C.,Starkuviene V.,Schlenczeck S.,Dencker S.,Huber R.,Klenk H.-P.,Kramer W.,Merkl R.,Gottschalk G.,Fritz H.-J.
The genome sequence of the extreme thermophile Thermus thermophilus.
Nat. Biotechnol.
22
547-553
2004
302242
Miyazaki J.,Asada K.,Fushinobu S.,Kuzuyama T.,Nishiyama M.
Crystal structure of tetrameric homoisocitrate dehydrogenase from an extreme thermophile, Thermus thermophilus: involvement of hydrophobic dimer-dimer interaction in extremely high thermotolerance.
J. Bacteriol.
187
6779-6788
2005
302243
Suzuki Y.,Asada K.,Miyazaki J.,Tomita T.,Kuzuyama T.,Nishiyama M.
Enhancement of the latent 3-isopropylmalate dehydrogenase activity of promiscuous homoisocitrate dehydrogenase by directed evolution.
Biochem. J.
431
401-410
2010
302244
Takahashi K.,Tomita T.,Kuzuyama T.,Nishiyama M.
Determinants of dual substrate specificity revealed by the crystal structure of homoisocitrate dehydrogenase from Thermus thermophilus in complex with homoisocitrate, Mg(2+) and NADH.
Biochem. Biophys. Res. Commun.
478
1688-1693
2016
