| Tag | Content |
|---|
| CPLM ID | CPLM-013300 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial |
Protein Synonyms/Alias | Dehydrogenase E1 and transketolase domain-containing protein 1 |
Gene Name | Dhtkd1 |
Gene Synonyms/Alias | |
Created Date | July 27, 2013 |
Organism | Rattus norvegicus (Rat) |
NCBI Taxa ID | 10116 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 553 | QLHSHLLKMYVQSRM | acetylation | [1] |
|
Reference | [1] Proteomic analysis of lysine acetylation sites in rat tissues reveals organ specificity and subcellular patterns. Lundby A, Lage K, Weinert BT, Bekker-Jensen DB, Secher A, Skovgaard T, Kelstrup CD, Dmytriyev A, Choudhary C, Lundby C, Olsen JV. Cell Rep. 2012 Aug 30;2(2):419-31. [ PMID: 22902405] |
Functional Description | 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) (By similarity). |
Sequence Annotation | |
Keyword | Complete proteome; Glycolysis; Mitochondrion; Oxidoreductase; Reference proteome; Thiamine pyrophosphate; Transit peptide. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 920 AA |
Protein Sequence | MASATVAAAG RALRRAVPLL RRSYQTERGV YGYRPRKAGS GEPRGDRARP SVDHGLARLV 60
TVYCEHGHKA AQINPLFPGQ ALLDTVPEIQ ALVQTLQGPF TTTGLLNMGK EEASLEEVLA 120
YLNHIYCGPI SIETAQLQSQ EEKDWFARRF EELKKETFTT EERKHLSKLL LESQEFDHFL 180
ATKFATVKRY GGEGAESMMG FFHELLKLSA YGGITDIIIG MPHRGRLNLL TGLLQLPPEL 240
MFRKMRGLSE FPENVAAIGD VLSHLTSSVD LDFGAHRPLH VTMLPNPSHL EAINPVAVGK 300
TRGRQQSQED GDYSPNGSAQ PGDKVICLQV HGDASFCGQG IVLETFTLSN LPHFRIGGSI 360
HLIVNNQLGY TTPAERGRSS LYSSDIGKLV GCAIIHVNGD SPEEVVRATR LAFEYQRQFR 420
KDVIIDLLCY RQWGHNELDE PFFTNPVMYK IIRARKSIPD TYAEHLIASG LMTQEEVSDI 480
KASYYAKLNG HLANVAHYSP PAPHLQARWQ GLVQPAACVT TWDTGVPLEL LRFVGVKSVE 540
VPEELQLHSH LLKMYVQSRM EKVKNGTNLD WATAETLALG SLLAQGFNVR LSGQDVGRGT 600
FSQRHAMVVC QNTDDVYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL 660
WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGLVILLPHG YDGAGPDHSS CRIERFLQMC 720
DSAEEGVDSD TVNMFVVHPT TPAQYFHLLR RQMMRNFRKP LIVASPKMLL RYPVAVSTLE 780
EMAPGTAFKP VIGDSSVDPK NVKTLIFCSG KHFYALLKQR ESLGAKKRDF AIIRLEELCP 840
FPLDSLQQEM GKYKHVQDII WSQEEPQNMG PWSFVYPRFE KQLACKLRLV SRPPLPAPAV 900
GIGTVHQQQH EAILFKTFTS 920 |
Gene Ontology | GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell. GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:EC. GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. GO:0006096; P:glycolysis; IEA:UniProtKB-KW. GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. |
Interpro | |
Pfam | |
SMART | |
PROSITE | |
PRINTS | |