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Database: UniProt
Entry: ODO1_BACSU
LinkDB: ODO1_BACSU
Original site: ODO1_BACSU 
ID   ODO1_BACSU              Reviewed;         944 AA.
AC   P23129; O68261; Q45642;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   28-JUL-2009, sequence version 3.
DT   07-JUN-2017, entry version 131.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=odhA; Synonyms=citK; OrderedLocusNames=BSU19370;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=1508153; DOI=10.1007/BF00283849;
RA   Resnekov O., Melin L., Carlsson P., Mannerloev M., von Gabain A.,
RA   Hederstedt L.;
RT   "Organization and regulation of the Bacillus subtilis odhAB operon,
RT   which encodes two of the subenzymes of the 2-oxoglutarate
RT   dehydrogenase complex.";
RL   Mol. Gen. Genet. 234:285-296(1992).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION.
RX   PubMed=10568751; DOI=10.1101/gr.9.11.1116;
RA   Medigue C., Rose M., Viari A., Danchin A.;
RT   "Detecting and analyzing DNA sequencing errors: toward a higher
RT   quality of the Bacillus subtilis genome sequence.";
RL   Genome Res. 9:1116-1127(1999).
RN   [4]
RP   SEQUENCE REVISION.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA   Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus
RT   subtilis 168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-270.
RC   STRAIN=168;
RX   PubMed=9734814; DOI=10.1093/dnares/5.3.195;
RA   Ghim S.-Y., Choi S.-K., Shin B.-S., Jeong Y.-M., Sorokin A.,
RA   Ehrlich S.D., Park S.-H.;
RT   "Sequence analysis of the Bacillus subtilis 168 chromosome region
RT   between the sspC and odhA loci (184 degrees-180 degrees).";
RL   DNA Res. 5:195-201(1998).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 652-944.
RC   STRAIN=168;
RX   PubMed=2500417; DOI=10.1128/jb.171.7.3667-3672.1989;
RA   Carlsson P., Hederstedt L.;
RT   "Genetic characterization of Bacillus subtilis odhA and odhB, encoding
RT   2-oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase,
RT   respectively.";
RL   J. Bacteriol. 171:3667-3672(1989).
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:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC   -!- SUBUNIT: Homodimer.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family. {ECO:0000305}.
DR   EMBL; X54805; CAA38576.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13829.3; -; Genomic_DNA.
DR   EMBL; AF026147; AAC17864.1; -; Genomic_DNA.
DR   EMBL; M27141; AAA22628.1; -; Genomic_DNA.
DR   PIR; S25295; A32879.
DR   RefSeq; NP_389819.3; NC_000964.3.
DR   RefSeq; WP_004399330.1; NZ_JNCM01000036.1.
DR   ProteinModelPortal; P23129; -.
DR   SMR; P23129; -.
DR   PRIDE; P23129; -.
DR   EnsemblBacteria; CAB13829; CAB13829; BSU19370.
DR   GeneID; 939507; -.
DR   KEGG; bsu:BSU19370; -.
DR   PATRIC; fig|224308.179.peg.2118; -.
DR   HOGENOM; HOG000259588; -.
DR   InParanoid; P23129; -.
DR   KO; K00164; -.
DR   OMA; IDMVCYR; -.
DR   PhylomeDB; P23129; -.
DR   BioCyc; BSUB:BSU19370-MONOMER; -.
DR   Proteomes; UP000001570; 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   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
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   Complete proteome; Glycolysis; Oxidoreductase; Reference proteome;
KW   Thiamine pyrophosphate.
FT   CHAIN         1    944       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162169.
FT   CONFLICT     35     35       N -> Y (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    110    110       L -> S (in Ref. 5; AAC17864).
FT                                {ECO:0000305}.
FT   CONFLICT    133    133       P -> L (in Ref. 5; AAC17864).
FT                                {ECO:0000305}.
FT   CONFLICT    231    231       I -> T (in Ref. 5; AAC17864).
FT                                {ECO:0000305}.
FT   CONFLICT    275    277       NKD -> RS (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    283    316       GSIGISYGWTGDVKYHLGANRELQDAETKSARIT -> DPL
FT                                ESATDGRGMSNTIWGRIGSFKTLKQNQPALP (in Ref.
FT                                1; CAA38576). {ECO:0000305}.
FT   CONFLICT    488    494       VKQIFAE -> SNKFSLK (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    520    522       DAY -> VAI (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    554    556       DFD -> HFH (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    567    569       NWP -> TG (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    573    585       NVFGKLKRILERR -> MFSQAKAHFRKT (in Ref. 1;
FT                                CAA38576). {ECO:0000305}.
FT   CONFLICT    837    838       SD -> DV (in Ref. 6; AAA22628).
FT                                {ECO:0000305}.
FT   CONFLICT    838    838       D -> V (in Ref. 1; CAA38576).
FT                                {ECO:0000305}.
FT   CONFLICT    927    944       VHKKEQERIVSDSLTRKN -> EFIKKNRNVLYLIA (in
FT                                Ref. 1; CAA38576). {ECO:0000305}.
SQ   SEQUENCE   944 AA;  106278 MW;  DCBC7B28C44A9CC2 CRC64;
     MFQNSMKQRM NWEDFYGPNL GYALELYDQY TQDPNSIDPD LKEMFDELGA PPSDIKEASG
     TKEKGRVTAD LIQKIASAVR LAEDIRTYGH LNASVNPLRK DEKKSELFPL SDYGLTEEEI
     KAIPASVICK DAPKNISNGL EAIQYLRNTY KRTISFEFDH VHDFKEREWL TRKIESGELF
     QKNSAEKLSA VLERLTEVEG FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKSGTT
     SVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSIGISYG WTGDVKYHLG
     ANRELQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQSGYPVQ DETKSLAILI
     HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF TTESAESRST KYASDLAKGY
     EIPIVHVNAD DPEACLSAVK FAVEYRKTFN KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD
     AVRKHPTVKQ IFAEKLVKEG VVTEEVVQNI EKSVTKRIED AYQKVPSKKE HTACEIELPE
     PVSNGFPDVD TSIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA
     ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG KEFVPLHHLS DCSTSFAVHN
     SPLSEGSVLG FEYGYNVHSP ETLVLWEAQY GDFANAAQVY FDQFISAGRA KWGQKSGLVM
     LLPHGYEGQG PEHSSGRIER FLQLAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL
     VIMTPKSLLR NPNTVSEVQE LSESRFQPVY EQSGLSHDYE KVTRLVLSSG KVSIDISDHF
     NKLEDGKEWL HIARIEQLYP FPAKGVKELF AKLPNLKEIV WVQEEPQNMG AWGYISPYLT
     EIAPEGVSVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN
//
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