Identification |
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Name | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial |
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Synonyms | - 2-oxoglutarate dehydrogenase complex component E2
- OGDC-E2
- Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex
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Gene Name | KGD2 |
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Enzyme Class | |
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Biological Properties |
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General Function | Involved in acyltransferase activity |
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Specific Function | The 2-oxoglutarate dehydrogenase complex catalyzes the overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It contains multiple copies of three enzymatic components:2- oxoglutarate dehydrogenase (E1), dihydrolipoamide succinyltransferase (E2) and lipoamide dehydrogenase (E3) |
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Cellular Location | Mitochondrion |
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SMPDB Pathways | Not Available |
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KEGG Pathways | |
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SMPDB Reactions | Not Available |
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KEGG Reactions | Not Available |
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Metabolites | YMDB ID | Name | View |
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YMDB00045 | Coenzyme A | Show | YMDB00514 | Succinyl-CoA | Show |
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GO Classification | Component |
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macromolecular complex | protein complex | oxoglutarate dehydrogenase complex | Function |
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transferase activity, transferring acyl groups | transferase activity, transferring acyl groups other than amino-acyl groups | acyltransferase activity | S-acyltransferase activity | S-succinyltransferase activity | catalytic activity | dihydrolipoyllysine-residue succinyltransferase activity | transferase activity | Process |
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cellular metabolic process | cofactor metabolic process | coenzyme metabolic process | acetyl-CoA metabolic process | acetyl-CoA catabolic process | tricarboxylic acid cycle | metabolic process |
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Gene Properties |
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Chromosome Location | chromosome 4 |
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Locus | YDR148C |
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Gene Sequence | >1392 bp
ATGCTTTCCAGAGCGACGCGTACTGCAGCTGCCAAATCCTTAGTAAAATCTAAAGTGGCT
AGAAATGTTATGGCTGCTTCTTTCGTCAAGAGACATGCTTCTACAAGTTTGTTCAAACAA
GCTAACAAGGTCGAATCCTTAGGTTCAATATATTTATCCGGCAAGAAAATTTCAGTTGCG
GCGAATCCGTTCTCCATAACTAGCAATCGTTTTAAATCTACCTCTATTGAAGTTCCTCCG
ATGGCAGAGTCCCTGACTGAAGGCTCTTTAAAGGAATATACTAAAAACGTTGGTGATTTT
ATTAAGGAGGACGAGCTGTTGGCCACTATTGAGACCGATAAAATTGATATTGAGGTCAAT
TCGCCAGTATCAGGTACTGTTACGAAGCTAAATTTCAAACCAGAGGACACTGTCACTGTT
GGTGAGGAGTTAGCTCAGGTCGAGCCTGGTGAAGCACCTGCTGAGGGTTCTGGAGAATCT
AAGCCAGAGCCTACCGAACAAGCGGAGCCATCGCAAGGTGTCGCCGCAAGGGAAAACTCA
AGTGAGGAAACGGCTTCAAAGAAAGAAGCTGCTCCAAAGAAAGAAGCCGCTCCAAAGAAA
GAAGTTACAGAACCAAAAAAGGCTGATCAACCAAAGAAGACCGTCTCTAAGGCGCAGGAA
CCCCCAGTAGCCTCTAACTCTTTCACACCATTTCCACGTACAGAAACCAGGGTCAAAATG
AACCGTATGAGATTGAGGATTGCCGAAAGATTAAAAGAGTCTCAAAACACTGCTGCTTCC
TTAACCACATTCAACGAAGTTGACATGTCAGCTTTGATGGAAATGAGGAAACTGTATAAA
GATGAGATTATTAAGAAGACCGGTACTAAATTCGGATTCATGGGTCTTTTCTCCAAAGCA
TGTACCTTGGCCGCCAAGGATATTCCAGCCGTCAATGGTGCCATTGAAGGTGACCAGATT
GTTTATCGTGATTACACAGATATTTCTGTTGCTGTGGCCACTCCAAAGGGTTTGGTTACC
CCCGTCGTTCGTAATGCAGAGTCATTGAGTGTTTTAGATATTGAGAACGAAATTGTTCGC
TTGAGTCATAAAGCGCGTGATGGCAAATTAACCCTAGAAGATATGACGGGTGGTACTTTC
ACCATATCTAATGGTGGTGTTTTTGGTTCATTATACGGTACTCCTATCATCAATTCACCA
CAAACAGCCGTCCTAGGCTTGCATGGTGTCAAAGAGAGACCTGTCACTGTTAATGGACAA
ATTGTCTCAAGACCAATGATGTACTTGGCTTTGACTTATGATCATAGATTGCTAGATGGT
AGAGAAGCTGTTACCTTCTTGAAGACTGTTAAAGAGTTGATTGAAGACCCTAGAAAAATG
TTGTTATGGTGA |
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Protein Properties |
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Pfam Domain Function | |
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Protein Residues | 463 |
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Protein Molecular Weight | 50430.30078 |
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Protein Theoretical pI | 9.44 |
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Signalling Regions | |
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Transmembrane Regions | |
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Protein Sequence | >Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial
MLSRATRTAAAKSLVKSKVARNVMAASFVKRHASTSLFKQANKVESLGSIYLSGKKISVA
ANPFSITSNRFKSTSIEVPPMAESLTEGSLKEYTKNVGDFIKEDELLATIETDKIDIEVN
SPVSGTVTKLNFKPEDTVTVGEELAQVEPGEAPAEGSGESKPEPTEQAEPSQGVAARENS
SEETASKKEAAPKKEAAPKKEVTEPKKADQPKKTVSKAQEPPVASNSFTPFPRTETRVKM
NRMRLRIAERLKESQNTAASLTTFNEVDMSALMEMRKLYKDEIIKKTGTKFGFMGLFSKA
CTLAAKDIPAVNGAIEGDQIVYRDYTDISVAVATPKGLVTPVVRNAESLSVLDIENEIVR
LSHKARDGKLTLEDMTGGTFTISNGGVFGSLYGTPIINSPQTAVLGLHGVKERPVTVNGQ
IVSRPMMYLALTYDHRLLDGREAVTFLKTVKELIEDPRKMLLW |
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References |
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External Links | |
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General Reference | - Repetto, B., Tzagoloff, A. (1990). "Structure and regulation of KGD2, the structural gene for yeast dihydrolipoyl transsuccinylase." Mol Cell Biol 10:4221-4232.2115121
- Jacq, C., Alt-Morbe, J., Andre, B., Arnold, W., Bahr, A., Ballesta, J. P., Bargues, M., Baron, L., Becker, A., Biteau, N., Blocker, H., Blugeon, C., Boskovic, J., Brandt, P., Bruckner, M., Buitrago, M. J., Coster, F., Delaveau, T., del Rey, F., Dujon, B., Eide, L. G., Garcia-Cantalejo, J. M., Goffeau, A., Gomez-Peris, A., Zaccaria, P., et, a. l. .. (1997). "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV." Nature 387:75-78.9169867
- Ghaemmaghami, S., Huh, W. K., Bower, K., Howson, R. W., Belle, A., Dephoure, N., O'Shea, E. K., Weissman, J. S. (2003). "Global analysis of protein expression in yeast." Nature 425:737-741.14562106
- Reinders, J., Wagner, K., Zahedi, R. P., Stojanovski, D., Eyrich, B., van der Laan, M., Rehling, P., Sickmann, A., Pfanner, N., Meisinger, C. (2007). "Profiling phosphoproteins of yeast mitochondria reveals a role of phosphorylation in assembly of the ATP synthase." Mol Cell Proteomics 6:1896-1906.17761666
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