Sequence of AROE_CORGL
EC Number:1.1.1
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
283
29697
Reaction
Other sequences found for EC No. 1.1.1
EC Number:1.1.1.24
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
quinate/shikimate dehydrogenase (NAD+)
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
283
29697
Reaction
L-quinate + NAD+ = 3-dehydroquinate + NADH + H+
Other sequences found for EC No. 1.1.1.24
EC Number:1.1.1.25
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
shikimate dehydrogenase (NADP+)
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
283
29697
Reaction
shikimate + NADP+ = 3-dehydroshikimate + NADPH + H+
Other sequences found for EC No. 1.1.1.25
EC Number:1.1.1.282
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
quinate/shikimate dehydrogenase [NAD(P)+]
Q9X5C9
Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / BCRC 11384 / JCM 1318 / LMG 3730 / NCIMB 10025)
283
29697
Reaction
L-quinate + NAD(P)+ = 3-dehydroquinate + NAD(P)H + H+
Other sequences found for EC No. 1.1.1.282
General information:
Sequence
0 MNDSILLGLI GQGLDLSRTP AMHEAEGLAQ GRATVYRRID TLGSRASGQD LKTLLDAALY
60 LGFNGLNITH PYKQAVLPLL DEVSEQATQL GAVNTVVIDA TGHTTGHNTD VSGFGRGMEE
120 GLPNAKLDSV VQVGAGGVGN AVAYALVTHG VQKLQVADLD TSRAQALADV INNAVGREAV
180 VGVDARGIED VIAAADGVVN ATPMGMPAHP GTAFDVSCLT KDHWVGDVVY MPIETELLKA
240 ARALGCETLD GTRMAIHQAV DAFRLFTGLE PDVSRMRETF LSL
Download this sequence
in fasta formatDownload all sequences for 1.1.1.282
in fasta format
in csv (Excel, OpenOffice) formatSequence related references
Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
770239
Ikeda M.,Nakagawa S.
The Corynebacterium glutamicum genome: features and impacts on biotechnological processes.
Appl. Microbiol. Biotechnol.
62
99-109
2003
770240
Kalinowski J.,Bathe B.,Bartels D.,Bischoff N.,Bott M.,Burkovski A.,Dusch N.,Eggeling L.,Eikmanns B.J.,Gaigalat L.,Goesmann A.,Hartmann M.,Huthmacher K.,Kraemer R.,Linke B.,McHardy A.C.,Meyer F.,Moeckel B.,Pfefferle W.,Puehler A.,Rey D.A.,Rueckert C.,Rupp O.,Sahm H.,Wendisch V.F.,Wiegraebe I.,Tauch A.
The complete Corynebacterium glutamicum ATCC 13032 genome sequence and its impact on the production of L-aspartate-derived amino acids and vitamins.
J. Biotechnol.
104
5-25
2003
770241
Schoepe J.,Niefind K.,Schomburg D.
1.6 Angstroms structure of an NAD(+)-dependent quinate dehydrogenase from Corynebacterium glutamicum.
Acta Crystallogr. D
64
803-809
2008
770242
Hoppner A.,Schomburg D.,Niefind K.
Enzyme-substrate complexes of the quinate/shikimate dehydrogenase from Corynebacterium glutamicum enable new insights in substrate and cofactor binding, specificity, and discrimination.
Biol. Chem.
394
1505-1516
2013
