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   03-AUG-2022, entry version 127.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; OrderedLocusNames=CBU_1399;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
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=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella 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   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: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000250|UniProtKB:P0AFG3}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC         COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC         ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000250|UniProtKB:P0AFG3};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000250|UniProtKB:P0AFG3}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000305}.
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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; NC_002971.3.
DR   RefSeq; WP_010958201.1; NZ_CCYB01000027.1.
DR   AlphaFoldDB; P51056; -.
DR   SMR; P51056; -.
DR   STRING; 227377.CBU_1399; -.
DR   PRIDE; P51056; -.
DR   DNASU; 1209305; -.
DR   EnsemblBacteria; AAO90898; AAO90898; CBU_1399.
DR   GeneID; 1209305; -.
DR   KEGG; cbu:CBU_1399; -.
DR   PATRIC; fig|227377.7.peg.1401; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OMA; RDSYCRT; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-KW.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   Gene3D; 3.40.50.11610; -; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   PANTHER; PTHR23152; PTHR23152; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; SSF52518; 2.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..934
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_0000162190"
FT   CONFLICT        600
FT                   /note="A -> R (in Ref. 1; AAA61785)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        614..630
FT                   /note="VGQDSRRGTFFHRHAVV -> SVKIPDEALFFIAMPLW (in Ref. 1;
FT                   AAA61785)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        778..782
FT                   /note="PKSVL -> QKCA (in Ref. 1; AAA61785)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        809..816
FT                   /note="HDPKKITR -> RIRKKSPA (in Ref. 1; AAA61785)"
FT                   /evidence="ECO:0000305"
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