ID   ODO1_BACCZ              Reviewed;         955 AA.
AC   Q63EB1;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   16-JUN-2009, entry version 30.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; OrderedLocusNames=BCE33L1152;
OS   Bacillus cereus (strain ZK / E33L).
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=288681;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16621833; DOI=10.1128/JB.188.9.3382-3390.2006;
RA   Han C.S., Xie G., Challacombe J.F., Altherr M.R., Bhotika S.S.,
RA   Bruce D., Campbell C.S., Campbell M.L., Chen J., Chertkov O.,
RA   Cleland C., Dimitrijevic M., Doggett N.A., Fawcett J.J., Glavina T.,
RA   Goodwin L.A., Hill K.K., Hitchcock P., Jackson P.J., Keim P.,
RA   Kewalramani A.R., Longmire J., Lucas S., Malfatti S., McMurry K.,
RA   Meincke L.J., Misra M., Moseman B.L., Mundt M., Munk A.C.,
RA   Okinaka R.T., Parson-Quintana B., Reilly L.P., Richardson P.,
RA   Robinson D.L., Rubin E., Saunders E., Tapia R., Tesmer J.G.,
RA   Thayer N., Thompson L.S., Tice H., Ticknor L.O., Wills P.L.,
RA   Brettin T.S., Gilna P.;
RT   "Pathogenomic sequence analysis of Bacillus cereus and Bacillus
RT   thuringiensis isolates closely related to Bacillus anthracis.";
RL   J. Bacteriol. 188:3382-3390(2006).
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; CP000001; AAU19096.1; -; Genomic_DNA.
DR   RefSeq; YP_082751.1; -.
DR   GeneID; 3026301; -.
DR   GenomeReviews; CP000001_GR; BCE33L1152.
DR   KEGG; bcz:BCZK1152; -.
DR   HOGENOM; Q63EB1; -.
DR   OMA; Q63EB1; EGDEPAF.
DR   BioCyc; BCER288681:BCE33L1152-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_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   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    955       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162164.
SQ   SEQUENCE   955 AA;  106476 MW;  528E7E8C90512B82 CRC64;
     MTRKNTTTNP WAKFHGPNLG YVIEQYDLYV TGAGSVDPEL QELFEIFGAP SFQDDVVTGD
     NTATHFSPQN TGNIEKILKV VQLVEQIRSF GHTLAHINPM EDAANGQSLL ERAMNELSDA
     DLKAIPAKTV WQDAPEGIHT ALDVIHRLKE VYTQSLAYEF SHIQDSEERA WLHQMVESNS
     LRQPLSNKKR TALLKRLTAV EGFEQFLHKT FVGQKRFSIE GVDMLVPVLD EIVLEGAKNG
     VEDVMIGMAH RGRLSVLAHV LEKPYSHMFA EFKHAKIEGA VANSGWTGDV KYHLGREQVV
     SNEEVSTRVT LANNPSHLEF VNPVVEGFAR AAQENRKKSG LPEQDTSKSF VILVHGDAAF
     PGQGIVSETL NLSRLNAYQT GGTIHVIANN AVGFTTDSYD SRSTKYSSDL AKGFDIPIVH
     VNADDPEACL AAANLAIQYR MLFKKDFLID LIGYRRYGHN EMDDPAVTQP QVYKKIKNHP
     TVRAIYADQL QAAGVLNADE IETITQFTQE QLKSDYAQVP PADTSDATIH VKVPDVVAKG
     IQPIDTGVEL DSLRAINEGL LSWPEGFNVY PKVKKILERR KDALEENGKI EWALAESLAF
     ASILQEGTPI RLTGQDSQRG TFAHRHIVLH DTDTNETYSP LHRLPNINAS FSVHNSPLSE
     AAVVGYEYGY NVFAPETLVM WEAQYGDFSN TAQALFDQYV SAGRAKWGQK SGLVLLLPHG
     YEGQGPEHSS ARPERFLQLA AENNWTVANL TSAAQYFHIL RRQASILGTE AVRPLVLMTP
     KSLLRHPLTL STASQLSEGR FQPALEQENL GTKPNKVKRL VLSTGKMAID LAAEIESGKH
     EYNLDEIHIV RIEQLYPFPA EKVQSIIKRF KNLEEIIWVQ EEPRNMGAWH YMAPILFELA
     GDKVKTGYIG RPDRSSPSGG DPFAHKAEQE LIVAHALDVK YNFRQDKLEI EVFSN
//