ID   ODO1_CAEEL              Reviewed;        1029 AA.
AC   O61199;
DT   02-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 2.
DT   16-JUN-2009, entry version 57.
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   ORFNames=T22B11.5;
OS   Caenorhabditis elegans.
OC   Eukaryota; Metazoa; Nematoda; Chromadorea; Rhabditida; Rhabditoidea;
OC   Rhabditidae; Peloderinae; Caenorhabditis.
OX   NCBI_TaxID=6239;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bristol N2;
RX   MEDLINE=99069613; PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG   The C. elegans sequencing consortium;
RT   "Genome sequence of the nematode C. elegans: a platform for
RT   investigating biology.";
RL   Science 282:2012-2018(1998).
RN   [2]
RP   PROTEIN SEQUENCE OF 126-146; 297-317; 320-328; 372-391; 504-514;
RP   548-565; 622-633; 673-680; 910-918; 975-984 AND 992-1002, AND MASS
RP   SPECTROMETRY.
RA   Bienvenut W.V.;
RL   Submitted (MAR-2006) to UniProtKB.
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 matrix (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
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DR   EMBL; AF039040; AAB94185.2; -; Genomic_DNA.
DR   PIR; T15098; T15098.
DR   RefSeq; NP_500617.1; -.
DR   UniGene; Cel.17820; -.
DR   IntAct; O61199; 1.
DR   Ensembl; T22B11.5; Caenorhabditis elegans.
DR   GeneID; 177235; -.
DR   KEGG; cel:T22B11.5; -.
DR   NMPDR; fig|6239.3.peg.13185; -.
DR   WormBase; WBGene00020679; T22B11.5.
DR   WormPep; T22B11.5; CE28486.
DR   OMA; O61199; PRIRTTI.
DR   BRENDA; 1.2.4.2; 672.
DR   NextBio; 895922; -.
DR   ArrayExpress; O61199; -.
DR   GO; GO:0005759; C:mitochondrial matrix; IEA:UniProtKB-SubCell.
DR   GO; GO:0031966; C:mitochondrial membrane; ISS:UniProtKB.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; ISS:UniProtKB.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0009792; P:embryonic development ending in birth or eg...; IMP:WormBase.
DR   GO; GO:0006096; P:glycolysis; IEA:UniProtKB-KW.
DR   GO; GO:0040007; P:growth; IMP:WormBase.
DR   GO; GO:0002119; P:nematode larval development; IMP:WormBase.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   GO; GO:0040010; P:positive regulation of growth rate; IMP:WormBase.
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   1: Evidence at protein level;
KW   Complete proteome; Direct protein sequencing; Glycolysis;
KW   Mitochondrion; Oxidoreductase; Thiamine pyrophosphate;
KW   Transit peptide.
FT   TRANSIT       1      ?       Mitochondrion.
FT   CHAIN         ?   1029       2-oxoglutarate dehydrogenase E1
FT                                component, mitochondrial.
FT                                /FTId=PRO_0000234100.
SQ   SEQUENCE   1029 AA;  115661 MW;  71ECB0F4236135F4 CRC64;
     MHRASLICRL ASPSRINAIR NASSGKSHIS ASTLVQHRNQ SVAAAVKHEP FLNGSSSIYI
     EQMYEAWLQD PSSVHTSWDA YFRNVEAGAG PGQAFQAPPA TAYAGALGVS PAAAQVTTSS
     APATRLDTNA SVQSISDHLK IQLLIRSYQT RGHNIADLDP LGINSADLDD TIPPELELSF
     YGLGERDLDR EFLLPPTTFI SEKKSLTLRE ILQRLKDIYC TSTGVEYMHL NNLEQQDWIR
     RRFEAPRVTE LSHDQKKVLF KRLIRSTKFE EFLAKKWPSE KRFGLEGCEV LIPAMKQVID
     SSSTLGVDSF VIGMPHRGRL NVLANVCRQP LATILSQFST LEPADEGSGD VKYHLGVCIE
     RLNRQSQKNV KIAVVANPSH LEAVDPVVMG KVRAEAFYAG DEKCDRTMAI LLHGDAAFAG
     QGVVLETFNL DDLPSYTTHG AIHIVVNNQI GFTTDPRSSR SSPYCTDVGR VVGCPIFHVN
     VDDPEAVMHV CNVAADWRKT FKKDVIVDLV CYRRHGHNEL DEPMFTQPLM YQRIKQTKTA
     LEKYQEKILN EGVANEQYVK EELTKYGSIL EDAYENAQKV TYVRNRDWLD SPWDDFFKKR
     DPLKLPSTGI EQENIEQIIG KFSQYPEGFN LHRGLERTLK GRQQMLKDNS LDWACGEALA
     FGSLLKEGIH VRLSGQDVQR GTFSHRHHVL HDQKVDQKIY NPLNDLSEGQ GEYTVCNSSL
     SEYAVLGFEL GYSMVDPNSL VIWEAQFGDF SNTAQCIIDQ FISSGQSKWI RQSGLVMLLP
     HGYEGMGPEH SSARPERFLQ MCNEDDEIDL EKIAFEGTFE AQQLHDTNWI VANCTTPANI
     YHLLRRQVTM PFRKPAVVFS PKSLLRHPMA RSPVEDFQSG SNFQRVIPET GAPSQNPPDV
     KRVVFCTGKV YYDMVAARKH VGKENDVALV RVEQLSPFPY DLVQQECRKY QGAEILWAQE
     EHKNMGAWSF VQPRINSLLS IDGRATKYAG RLPSSSPATG NKFTHMQEQK EMMSKVFGVP
     KSKLEGFKA
//