Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial (P19262)
Identification | ||||||||||||||||||||||
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Name | Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial | |||||||||||||||||||||
Synonyms |
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Gene Name | KGD2 | |||||||||||||||||||||
Enzyme Class | ||||||||||||||||||||||
Biological Properties | ||||||||||||||||||||||
General Function | Involved in acyltransferase activity | |||||||||||||||||||||
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) | |||||||||||||||||||||
Cellular Location | Mitochondrion | |||||||||||||||||||||
SMPDB Pathways | Not Available | |||||||||||||||||||||
KEGG Pathways |
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SMPDB Reactions | Not Available | |||||||||||||||||||||
KEGG Reactions | Not Available | |||||||||||||||||||||
Metabolites |
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GO Classification |
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Gene Properties | ||||||||||||||||||||||
Chromosome Location | chromosome 4 | |||||||||||||||||||||
Locus | YDR148C | |||||||||||||||||||||
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 | |||||||||||||||||||||
Protein Properties | ||||||||||||||||||||||
Pfam Domain Function | ||||||||||||||||||||||
Protein Residues | 463 | |||||||||||||||||||||
Protein Molecular Weight | 50430.30078 | |||||||||||||||||||||
Protein Theoretical pI | 9.44 | |||||||||||||||||||||
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 | |||||||||||||||||||||
References | ||||||||||||||||||||||
External Links |
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General Reference |
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