ID   ODO1_GEOKA              Reviewed;         950 AA.
AC   Q5L172;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   04-NOV-2008, entry version 26.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=GK1023;
OS   Geobacillus kaustophilus.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1462;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HTA426;
RX   PubMed=15576355; DOI=10.1093/nar/gkh970;
RA   Takami H., Takaki Y., Chee G.-J., Nishi S., Shimamura S., Suzuki H.,
RA   Matsui S., Uchiyama I.;
RT   "Thermoadaptation trait revealed by the genome sequence of
RT   thermophilic Geobacillus kaustophilus.";
RL   Nucleic Acids Res. 32:6292-6303(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   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
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DR   EMBL; BA000043; BAD75308.1; -; Genomic_DNA.
DR   RefSeq; YP_146876.1; -.
DR   GeneID; 3184920; -.
DR   GenomeReviews; BA000043_GR; GK1023.
DR   KEGG; gka:GK1023; -.
DR   NMPDR; fig|235909.3.peg.1939; -.
DR   HOGENOM; Q5L172; -.
DR   BioCyc; GKAU235909:GK1023-MON; -.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:HAMAP.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01169; -; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DHase_E1.
DR   InterPro; IPR001017; DHase_E1.
DR   InterPro; IPR005475; Transketo_Cen_R.
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   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    950       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162172.
SQ   SEQUENCE   950 AA;  107561 MW;  0A9769B6BB8BC10F CRC64;
     MAKQTNYAQP WSQFYGPNLG YVIEMYEQYL DDPNSIDPEL KQLFEQWGAP VLEEPVSPAD
     DETAKTHQTF RLPETPTIFS KLVAAVKLAD SIRHYGHLVA DTNPLVKKEK KLRRLELDEY
     DLTEEDLKRI PVAFLCPHAP AHVKNGWDAI LHLRKIYTDK IAFEFSQVHN LEERNWLIQQ
     IESGAYYPSL ANKERVALLR RLTEVEGFEK FIHRTYVGQK RFSIEGLDSM VPLLDELVRQ
     AIEHEIDAVN IGMAHRGRLN VLAHVLGKPY EMIFAEFQHA ESKNFIPSEG SVAITYGWTG
     DVKYHLGAAR RLRNQSAHTM RITLANNPSH LEVVNPVVLG YTRAAQEDRT KPGVPVQNTD
     ASFAILIHGD AAFPGQGIVA ETLNLSQLRG YTTGGTIHII ANNMIGFTTE SYDSRSTTYA
     SDMAKGFEVP IVHVNADDPE ACLAAACLAF AYRQRFKKDF VIDLIGYRRF GHNEMDEPMA
     TNPTMYAIIN QHPTVRKLYA QKLMEKGIIT EREVDEMEQE VAERLKIAYE RVPKNEDELD
     FIMDPPKPVV DRLPEVKTSV AKDVLHRVNE ELLQFPDGFN VFNKLERILK RRSGVFAQNG
     KVDWAHAEIL AFATILQDGV PIRLTGQDSQ RGTFAQRHLV LHDVKTGEEY VPLHHISGAK
     ASFVVYNSPL TEAAVLGYEY GYNVYAPETL VLWEAQFGDF ANMAQVMFDQ FISSGRAKWG
     QKSGLVMLLP HGYEGQGPEH SSGRVERFLQ LAAENNWTVA NLSTAAQYFH ILRRQAALLT
     REEVRPLIIM TPKSLLRHPL AASDAEVFVD GAFSPVLEQP GLGADAGKVE RIVFGTGKLM
     IDLAEQIGKM ESLDWLHIVR IEELYPFPEE AVKDIIARYP NVKELVWVQE EPKNMGAWLY
     MEPRLRALAP EGVDVSYIGR RRRASPAEGD PVVHRKEQER IIRCALTKHE
//