ID ODO1_COXBU Reviewed; 934 AA. AC P51056; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 09-MAY-2003, sequence version 3. DT 25-NOV-2008, entry version 61. DE RecName: Full=2-oxoglutarate dehydrogenase E1 component; DE EC=1.2.4.2; DE AltName: Full=Alpha-ketoglutarate dehydrogenase; GN Name=sucA; OrderedLocusNames=CBU_1399; OS Coxiella burnetii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; OC Coxiellaceae; Coxiella. OX NCBI_TaxID=777; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Nine Mile; RA Schimmels J.A., Mallavia L.P.; RL Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=Nine Mile phase I; RA Thiele D., Willems H., Oswald W., Krauss H.; RL Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=Nine Mile phase I / RSA 493; RX MEDLINE=22608657; PubMed=12704232; DOI=10.1073/pnas.0931379100; RA Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., RA Nelson W.C., Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., RA DeBoy R.T., Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., RA Khouri H.M., Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., RA Thompson H.A., Samuel J.E., Fraser C.M., Heidelberg J.F.; RT "Complete genome sequence of the Q-fever pathogen, Coxiella RT burnetii."; RL Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-280. RC STRAIN=Nine Mile; RX MEDLINE=95212926; PubMed=7698664; DOI=10.1016/0378-1119(94)00888-Y; RA Heinzen R.A., Mo Y.-Y., Robertson S.J., Mallavia L.P.; RT "Characterization of the succinate dehydrogenase-encoding gene cluster RT (sdh) from the rickettsia Coxiella burnetii."; RL Gene 155:27-34(1995). 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). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + [dihydrolipoyllysine-residue CC succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue CC succinyltransferase] S-succinyldihydrolipoyllysine + CO(2). CC -!- COFACTOR: Thiamine pyrophosphate. CC -!- SUBUNIT: Homodimer (By similarity). CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase CC family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U07789; AAA61785.1; -; Unassigned_DNA. DR EMBL; X77919; CAA54874.1; -; Genomic_DNA. DR EMBL; AE016828; AAO90898.1; -; Genomic_DNA. DR EMBL; L33409; AAA74135.1; -; Genomic_DNA. DR PIR; S42874; S42874. DR RefSeq; NP_820384.1; -. DR GeneID; 1209305; -. DR GenomeReviews; AE016828_GR; CBU_1399. DR KEGG; cbu:CBU_1399; -. DR NMPDR; fig|227377.1.peg.1328; -. DR TIGR; CBU_1399; -. DR HOGENOM; P51056; -. DR BioCyc; CBUR227377:CBU_1399-MON; -. DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:InterPro. DR GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:InterPro. DR GO; GO:0006096; P:glycolysis; IEA:InterPro. DR GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW. 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 1 934 2-oxoglutarate dehydrogenase E1 FT component. FT /FTId=PRO_0000162190. FT CONFLICT 600 600 A -> R (in Ref. 1; AAA61785). FT CONFLICT 614 630 VGQDSRRGTFFHRHAVV -> SVKIPDEALFFIAMPLW FT (in Ref. 1; AAA61785). FT CONFLICT 778 782 PKSVL -> QKCA (in Ref. 1; AAA61785). FT CONFLICT 809 816 HDPKKITR -> RIRKKSPA (in Ref. 1; FT AAA61785). SQ SEQUENCE 934 AA; 106723 MW; 7FB8144F8E013E8D CRC64; MPKITMQQFQ KNSYLADNNA GYIETLYENF LKDPHSVNEE WRSYFRTLTN GASTPDISHA TIREEFRELA RKPRSISPTA ITPAAEQAAV DLLIEGYRRF GHLNAKINPL GDNRPVDSRL ELGHYNLTES DFNKTFATYG LLNKPKATLK EIYTRLREIY CGSIGVQYST ISDERERNWL RDYVEQRLPS IEFDKETKRN ILQQLVTAES LEKYLDTKYV GQVRYSLEGG DSLIPLLDEL TKRARHQKIE EIVICMAHRG RVNVLLNIMG QSAAELFQEF EGKKDYGLMS GDVKYHRGYS RDVKTDAGPI HLSLAFNPSH LEFICPVAMG SVRARQERQN GHKRDYAMTV MIHGDASFSG EGIVMEALSM SQTRAHHVGG SIHIILNNQV GFTTSNPHDA RSSMYCSDIA KMLDAPVFHV NGDDPEAVVA VTQLALDYRM AFHKDVFIDL VCYRRHGHQE VDDPMPTQPA MYKVIQEHPT TRTLYAKNLI EKKLCTAEEV DQWIDDYRDR LDRGRQLVET LPEGLSAHYA ANWTPYLGQD WTTLVDTTLP LKKLKALGKK FSTLPNTLHL HRKVEAIYKA RLEMAEGKTP MDWGFAEMLA YASLLEEGFS VRLVGQDSRR GTFFHRHAVV FDQETGKEYE PLKHLSDKQA APHIYDSLLC EAGALGFEYG YSTADPNSLV IWEAQFGDFA NVAQVIVDQF ISSGWQKWNR LSGIVLFLPH GYEGKGPEHS SARLERYLQL CAQNNMQVCA PTTPSQIFHL LRRQVLRPYR KPLVVLTPKS VLRNKLAVSS LEDLARGQLK LLIPEIEKHD PKKITRVILC SGKVYYDLLA KRREHKGKLN HIAMIRIEQL YPFPYDELKA ELEKYPNAKQ VIWCQEEPKN QGAWFCTRHR LIKCMRDDQT LEYVGRSAFA APAAGYSALY VKLQEQLVNQ ALEI //