Sequence of ODO2_AZOVI
EC Number:2.3.1.61
EC Number
Recommended Name
Accession Code
Organism
No of amino acids
Molecular Weight [Da]
Source
Reaction
succinyl-CoA + enzyme N6-(dihydrolipoyl)lysine = CoA + enzyme N6-(S-succinyldihydrolipoyl)lysine
Other sequences found for EC No. 2.3.1.61
General information:
Sequence
0 MAIDIKAPTF PESIADGTVA TWHKKPGEPV KRDELIVDIE TDKVVMEVLA EADGVIAEIV
60 KNEGDTVLSG ELLGKLTEGG AATAAPAAAP APAAAAPAAA EAPILSPAAR KIAEENAIAA
120 DSITGTGKGG RVTKEDAVAA AEAKKSAPAG QPAPAATAAP LFAAGDRVEK RVPMTRLRAK
180 VAERLVEAQS SMAMLTTFNE VNMKPVMELR AKYKDLFEKT HNGVRLGFMS FFVKAAVEAL
240 KRQPGVNASI DGNDIVYHGY QDIGVAVSSD RGLVVPVLRN AEFMSLAEIE GGINEFGKKA
300 KAGKLTIEEM TGGTFTISNG GVFGSLLSTP IVNPPQTAIL GMHKIQERPM AVNGQVVILP
360 MMYLALSYDH RLIDGKEAVT FLVTMKDLLE DPARLLLDV
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Sequence Reference
Authors
Title
Journal
Volume
Pages
Year
PubMed ID
69585
Westphal A.H.,de Kok A.
The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. Molecular cloning and sequence analysis of the gene encoding the succinyltransferase component.
Eur. J. Biochem.
187
235-239
1990
69586
Westphal A.H.,de Kok A.
Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, organization and sequence analysis of the gene.
Eur. J. Biochem.
172
299-305
1988
69587
Schulze E.,Westphal A.H.,Hanemaaijer R.,de Kok A.
The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. Molecular cloning and sequence analysis of the gene encoding the 2-oxoglutarate dehydrogenase component.
Eur. J. Biochem.
187
229-234
1990
69588
Berg A.,Smits O.,de Kok A.,Vervoort J.
Sequential 1H and 15N nuclear magnetic resonance assignments and secondary structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. Evidence for high structural similarity with the lipoyl domain of the pyruvate dehydrogenase complex.
Eur. J. Biochem.
234
148-159
1995
69589
Berg A.,Vervoort J.,de Kok A.
Solution structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii.
J. Mol. Biol.
261
432-442
1996
