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 03-AUG-2022, entry version 149.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {ECO:0000250|UniProtKB:P0AFG3, ECO:0000255|HAMAP-Rule:MF_01169};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN Name=odhA {ECO:0000255|HAMAP-Rule:MF_01169}; Synonyms=citK;
GN 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, which
RT encodes two of the subenzymes of the 2-oxoglutarate dehydrogenase
RT 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., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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 quality of
RT 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., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 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., Ehrlich S.D.,
RA Park S.-H.;
RT "Sequence analysis of the Bacillus subtilis 168 chromosome region between
RT 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 2-
RT oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase,
RT respectively.";
RL J. Bacteriol. 171:3667-3672(1989).
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, ECO:0000255|HAMAP-Rule:MF_01169}.
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, ECO:0000255|HAMAP-
CC Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000250|UniProtKB:P0AFG3,
CC ECO:0000255|HAMAP-Rule:MF_01169};
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 ECO:0000255|HAMAP-Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01169, ECO:0000305}.
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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 AlphaFoldDB; P23129; -.
DR SMR; P23129; -.
DR STRING; 224308.BSU19370; -.
DR jPOST; P23129; -.
DR PRIDE; P23129; -.
DR EnsemblBacteria; CAB13829; CAB13829; BSU_19370.
DR GeneID; 939507; -.
DR KEGG; bsu:BSU19370; -.
DR PATRIC; fig|224308.179.peg.2118; -.
DR eggNOG; COG0567; Bacteria.
DR InParanoid; P23129; -.
DR OMA; RDSYCRT; -.
DR PhylomeDB; P23129; -.
DR BioCyc; BSUB:BSU19370-MON; -.
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:UniProtKB-UniRule.
DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR Gene3D; 3.40.50.11610; -; 1.
DR HAMAP; MF_01169; SucA_OdhA; 1.
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; IPR042179; KGD_C_sf.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR PANTHER; PTHR23152; PTHR23152; 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..944
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_0000162169"
FT REGION 914..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 917..944
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 35
FT /note="N -> Y (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 110
FT /note="L -> S (in Ref. 5; AAC17864)"
FT /evidence="ECO:0000305"
FT CONFLICT 133
FT /note="P -> L (in Ref. 5; AAC17864)"
FT /evidence="ECO:0000305"
FT CONFLICT 231
FT /note="I -> T (in Ref. 5; AAC17864)"
FT /evidence="ECO:0000305"
FT CONFLICT 275..277
FT /note="NKD -> RS (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 283..316
FT /note="GSIGISYGWTGDVKYHLGANRELQDAETKSARIT -> DPLESATDGRGMSN
FT TIWGRIGSFKTLKQNQPALP (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 488..494
FT /note="VKQIFAE -> SNKFSLK (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 520..522
FT /note="DAY -> VAI (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 554..556
FT /note="DFD -> HFH (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 567..569
FT /note="NWP -> TG (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 573..585
FT /note="NVFGKLKRILERR -> MFSQAKAHFRKT (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 837..838
FT /note="SD -> DV (in Ref. 6; AAA22628)"
FT /evidence="ECO:0000305"
FT CONFLICT 838
FT /note="D -> V (in Ref. 1; CAA38576)"
FT /evidence="ECO:0000305"
FT CONFLICT 927..944
FT /note="VHKKEQERIVSDSLTRKN -> EFIKKNRNVLYLIA (in Ref. 1;
FT CAA38576)"
FT /evidence="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
