ODO1_BACLD
ID ODO1_BACLD Reviewed; 944 AA.
AC Q65IH4; Q62TX6;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {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};
GN OrderedLocusNames=BLi02260, BL01452;
OS Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 /
OS NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=279010;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15383718; DOI=10.1159/000079829;
RA Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P.,
RA Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.;
RT "The complete genome sequence of Bacillus licheniformis DSM13, an organism
RT with great industrial potential.";
RL J. Mol. Microbiol. Biotechnol. 7:204-211(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375
RC / NCTC 10341 / NRRL NRS-1264 / Gibson 46;
RX PubMed=15461803; DOI=10.1186/gb-2004-5-10-r77;
RA Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J.,
RA Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B.,
RA Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A.,
RA Bolotin A., Lapidus A., Galleron N., Ehrlich S.D., Berka R.M.;
RT "Complete genome sequence of the industrial bacterium Bacillus
RT licheniformis and comparisons with closely related Bacillus species.";
RL Genome Biol. 5:R77.1-R77.12(2004).
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: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; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={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:0000255|HAMAP-
CC Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR EMBL; AE017333; AAU41140.1; -; Genomic_DNA.
DR EMBL; CP000002; AAU23783.1; -; Genomic_DNA.
DR RefSeq; WP_003182695.1; NC_006322.1.
DR AlphaFoldDB; Q65IH4; -.
DR SMR; Q65IH4; -.
DR STRING; 279010.BL01452; -.
DR EnsemblBacteria; AAU23783; AAU23783; BL01452.
DR GeneID; 66215737; -.
DR KEGG; bld:BLi02260; -.
DR KEGG; bli:BL01452; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OMA; RDSYCRT; -.
DR OrthoDB; 29166at2; -.
DR BioCyc; BLIC279010:BLI_RS11210-MON; -.
DR Proteomes; UP000000606; Chromosome.
DR Bgee; BL01452; Expressed in pharyngeal slit and 10 other tissues.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
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_0000162167"
FT REGION 914..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 106671 MW; 9E63C701C8847E39 CRC64;
MFQNSMKQRM TWEEFHGPNL GYVLELYDQY VKDPESLDAD LKEMFDELGA PPGDIRAASQ
KNEEADFTAG SIQKIASAVK LAEDIRTYGH LNASVNPLRK TQEKQELFPL AEYGLTEQDV
KKIPASVICK DAPKEVTNGL EAIQYLRNTY KKSISFEFDH VHIFEERNWL MKKIESGELF
TPKSKEKLVE VLRRLTEVES LEQFLHKTFV GQKRFSIEGL DALVPMLDDI IAKSVSAGTT
NVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSTGINYG WTGDVKYHLG
ANRQIQDEHT KTARIALANN PSHLEFIDPI VEGSTRAAQE TRTESGYPVQ DVKKSMAILI
HGDAAFPGEG IVAETLNLSQ LKGYQVGGAI HIIANNMIGF TTESNESRST KYASDLAKGF
EIPIVHVNAD DPEACLSAVQ LAVEYRMTFN KDFLIDLIGY RRFGHNEMDE PSATQPMLYD
AVRKHPTVKN IFAEKLIHKG IVDKETVGKI KDAVQKRLEE AYRKVPAKKE DMTHEIVLPE
PVSNGFPDVD TSVDFETLRK INQELVSWPE NFNVFDKLKR ILERRAKAFE DDRKVDWSLA
EAMAFASILK DGTPLRLTGQ DSERGTFAHR NLVLHDSKTG DEFIALHHLA DTKASFAVHN
SPLSEGSVLG FEYGYNVSSP ETMVIWEAQF GDFANAAQVY FDQFISAGRA KWGQKSGLVV
LLPHGYEGQG PEHSSGRTER FLQLAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL
IIMTPKSLLR NPNTVSEVQE LSNSSFKPVY EMSGLSHQYD KVTRLVLSSG KVSIDISDHF
NKMEGEKDWL HIARVEELYP FPAKHIKAIF SKLPNLEEIV WVQEEPQNMG AWNYIEPYLR
EVAPKDVKVR YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN
