ID   ODO1_BOVIN              Reviewed;        1023 AA.
AC   Q148N0;
DT   13-NOV-2007, integrated into UniProtKB/Swiss-Prot.
DT   22-AUG-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component, mitochondrial;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
DE   Flags: Precursor;
GN   Name=OGDH;
OS   Bos taurus (Bovine).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Laurasiatheria; Cetartiodactyla; Ruminantia;
OC   Pecora; Bovidae; Bovinae; Bos.
OX   NCBI_TaxID=9913;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=Hereford; TISSUE=Uterus;
RG   NIH - Mammalian Gene Collection (MGC) project;
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
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   -!- ENZYME REGULATION: Catabolite repressed (By similarity).
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
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DR   EMBL; BC118106; AAI18107.1; -; mRNA.
DR   IPI; IPI00687413; -.
DR   RefSeq; NP_001069498.1; -.
DR   UniGene; Bt.46406; -.
DR   Ensembl; ENSBTAG00000006029; Bos taurus.
DR   GeneID; 534599; -.
DR   KEGG; bta:534599; -.
DR   HOVERGEN; Q148N0; -.
DR   OMA; Q148N0; PRIRTTI.
DR   BRENDA; 1.2.4.2; 251.
DR   GO; GO:0005759; C:mitochondrial matrix; 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; Isopeptide bond; Mitochondrion; Oxidoreductase;
KW   Thiamine pyrophosphate; Transit peptide; Ubl conjugation.
FT   TRANSIT       1     40       Mitochondrion (Potential).
FT   CHAIN        41   1023       2-oxoglutarate dehydrogenase E1
FT                                component, mitochondrial.
FT                                /FTId=PRO_0000310981.
FT   CROSSLNK    534    534       Glycyl lysine isopeptide (Lys-Gly)
FT                                (interchain with G-Cter in ubiquitin) (By
FT                                similarity).
SQ   SEQUENCE   1023 AA;  115808 MW;  46C5D3161D41F551 CRC64;
     MFHLRTCAAK LRPLTASQTV KTFSQNRPAA ARTFGQIRCY TAPVAAEPFL SGTSSNYVEE
     MYYAWLENPK SVHKSWDIFF RNTNAGAPPG TAYQSPLPLS PGSLSAVARA GPLVEAQPNV
     DKLVEDHLAV QSLIRAYQIR GHHVAQLDPL GILDADLDSS VPADIISSTD KLGFYGLDES
     DLDKVFHLPT TTFIGGQESA LPLREIIRRL EMAYCQHIGV EFMFINDLEQ CQWIRQKFET
     PGVMQFTNEE KRTLLARLVR STRFEEFLQR KWSSEKRFGL EGCEVLIPAL KTIIDKSSEN
     GVDYVIMGMP HRGRLNVLAN VIRKELEQIF CQFDSKLEAA DEGSGDVKYH LGMYHRRINR
     VTDRNITLSL VANPSHLEAA DPVVMGKTKA EQFYCGDTEG KKVMSILLHG DAAFAGQGIV
     YETFHLSDLP SYTTHGTVHV VVNNQIGFTT DPRMARSSPY PTDVARVVNA PIFHVNSDDP
     EAVMYVCKVA AEWRSTFHKD VVVDLVCYRR NGHNEMDEPM FTQPLMYKQI RKQKPVLQKY
     AELLVSQGVV NQPEYEEEIS KYDKICEEAF ARSKDEKILH IKHWLDSPWP GFFTLDGQPR
     SMTCPSTGLT EDILTHIGNV ASSVPVEDFT IHGGLSRILK TRGELVKNRT VDWALAEYMA
     FGSLLKEGIH IRLSGQDVER GTFSHRHHVL HDQNVDKRTC IPMNHLWPNQ APYTVCNSSL
     SEYGVLGFEL GFAMASPNAL VLWEAQFGDF HNTAQCIIDQ FICPGQAKWV RQNGIVLLLP
     HGMEGMGPEH SSARPERFLQ MCNDDPDVLP DLKEANFDIN QLYDCNWVVV NCSTPGNFFH
     VLRRQILLPF RKPLIIFTPK SLLRHPEARS NFDEMLPGTH FQRVIPEDGP AAQNPGNVKR
     LLFCTGKVYY DLTRERKARD MVEQVAITRI EQLSPFPFDL LLQEVQKYPS AELAWCQEEH
     KNQGYYDYVK PRLRTTISRA KPVWYAGRDP AAAPATGNKK THLTELQRLL DTAFDLDAFK
     NFS
//