ID   DHTK1_RAT               Reviewed;         920 AA.
AC   Q4KLP0;
DT   23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
DE   RecName: Full=Probable 2-oxoglutarate dehydrogenase E1 component DHKTD1, mitochondrial;
DE            EC=1.2.4.2;
DE   AltName: Full=Dehydrogenase E1 and transketolase domain-containing protein 1;
DE   Flags: Precursor;
GN   Name=Dhtkd1;
OS   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi;
OC   Muroidea; Muridae; Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-
CC       oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC       succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion (Potential).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
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DR   EMBL; BC099075; AAH99075.1; -; mRNA.
DR   IPI; IPI00364925; -.
DR   RefSeq; NP_001020891.1; -.
DR   UniGene; Rn.13539; -.
DR   GeneID; 361272; -.
DR   KEGG; rno:361272; -.
DR   RGD; 1308092; Dhtkd1.
DR   HOVERGEN; Q4KLP0; -.
DR   BRENDA; 1.2.4.2; 248.
DR   NextBio; 675775; -.
DR   ArrayExpress; Q4KLP0; -.
DR   GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-SubCell.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:EC.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR005475; Transketolase_central-reg.
DR   PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   2: Evidence at transcript level;
KW   Glycolysis; Mitochondrion; Oxidoreductase; Thiamine pyrophosphate;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion (Potential).
FT   CHAIN         ?    920       Probable 2-oxoglutarate dehydrogenase E1
FT                                component DHKTD1, mitochondrial.
FT                                /FTId=PRO_0000307939.
SQ   SEQUENCE   920 AA;  102642 MW;  AA4A70E36AA41104 CRC64;
     MASATVAAAG RALRRAVPLL RRSYQTERGV YGYRPRKAGS GEPRGDRARP SVDHGLARLV
     TVYCEHGHKA AQINPLFPGQ ALLDTVPEIQ ALVQTLQGPF TTTGLLNMGK EEASLEEVLA
     YLNHIYCGPI SIETAQLQSQ EEKDWFARRF EELKKETFTT EERKHLSKLL LESQEFDHFL
     ATKFATVKRY GGEGAESMMG FFHELLKLSA YGGITDIIIG MPHRGRLNLL TGLLQLPPEL
     MFRKMRGLSE FPENVAAIGD VLSHLTSSVD LDFGAHRPLH VTMLPNPSHL EAINPVAVGK
     TRGRQQSQED GDYSPNGSAQ PGDKVICLQV HGDASFCGQG IVLETFTLSN LPHFRIGGSI
     HLIVNNQLGY TTPAERGRSS LYSSDIGKLV GCAIIHVNGD SPEEVVRATR LAFEYQRQFR
     KDVIIDLLCY RQWGHNELDE PFFTNPVMYK IIRARKSIPD TYAEHLIASG LMTQEEVSDI
     KASYYAKLNG HLANVAHYSP PAPHLQARWQ GLVQPAACVT TWDTGVPLEL LRFVGVKSVE
     VPEELQLHSH LLKMYVQSRM EKVKNGTNLD WATAETLALG SLLAQGFNVR LSGQDVGRGT
     FSQRHAMVVC QNTDDVYIPL NHMDPNQKGF LEVSNSPLSE EAVLGFEYGM SIESPKLLPL
     WEAQFGDFFN GAQIIFDTFI SGGEAKWLLQ SGLVILLPHG YDGAGPDHSS CRIERFLQMC
     DSAEEGVDSD TVNMFVVHPT TPAQYFHLLR RQMMRNFRKP LIVASPKMLL RYPVAVSTLE
     EMAPGTAFKP VIGDSSVDPK NVKTLIFCSG KHFYALLKQR ESLGAKKRDF AIIRLEELCP
     FPLDSLQQEM GKYKHVQDII WSQEEPQNMG PWSFVYPRFE KQLACKLRLV SRPPLPAPAV
     GIGTVHQQQH EAILFKTFTS
//