ID   ODO1_BACVZ              Reviewed;         944 AA.
AC   A7Z5J9;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   23-OCT-2007, sequence version 1.
DT   27-MAR-2024, entry version 99.
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=RBAM_019130;
OS   Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS   (Bacillus amyloliquefaciens subsp. plantarum).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus amyloliquefaciens group.
OX   NCBI_TaxID=326423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42;
RX   PubMed=17704766; DOI=10.1038/nbt1325;
RA   Chen X.H., Koumoutsi A., Scholz R., Eisenreich A., Schneider K.,
RA   Heinemeyer I., Morgenstern B., Voss B., Hess W.R., Reva O., Junge H.,
RA   Voigt B., Jungblut P.R., Vater J., Suessmuth R., Liesegang H.,
RA   Strittmatter A., Gottschalk G., Borriss R.;
RT   "Comparative analysis of the complete genome sequence of the plant growth-
RT   promoting bacterium Bacillus amyloliquefaciens FZB42.";
RL   Nat. Biotechnol. 25:1007-1014(2007).
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=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000255|HAMAP-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; CP000560; ABS74275.1; -; Genomic_DNA.
DR   RefSeq; WP_012117750.1; NC_009725.2.
DR   AlphaFoldDB; A7Z5J9; -.
DR   SMR; A7Z5J9; -.
DR   KEGG; bay:RBAM_019130; -.
DR   HOGENOM; CLU_004709_1_0_9; -.
DR   Proteomes; UP000001120; Chromosome.
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   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 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   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 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; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN           1..944
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="PRO_1000065696"
FT   REGION          915..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"
SQ   SEQUENCE   944 AA;  106267 MW;  936E7315F09C54CD CRC64;
     MFQNNMKQRM NWEDFYGPNL GYALELYDQY AEDPDSIDPD LKDMFDELGA PPSQIKEASG
     TKEQGRVTAD LIQKIAAAVK LAEDIRTYGH LNASVNPLRK DPKKSELFPL SDYGLTEEEM
     KAIPASVICK DAPANITNGL EAIQHLRNTY KRTISFEFDH VHDFEERAWI TKMVESGELF
     RKNSPEKLSA VLERLTEVEG FEQFLHRTFV GQKRFSIEGL DALVPVLDDI IAQSVKAGTT
     NVNIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKDLVP SEGSTGISYG WTGDVKYHLG
     ADRQLQDAET KSARITLANN PSHLEFINPI VEGSTRAAQE TRTQKGYPVQ DETKSLAILI
     HGDAAFPGEG IVAETLNLSS LKGYQVGGAI HIIANNMIGF TTESDESRST KYASDLAKGY
     EIPIVHVNAD DPEACLSAVK FAVEYRKRFN KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD
     AVRKHPTVKR IFAEKLVSEG LISEEKAQNI ETAVTKRIED AYKKVPAKKE DAVREIELPE
     PVSNGFPDVD TAIDFDVLRK LNGELINWPE SFNVFGKLKR ILERRAKAFD DDRKVEWSLA
     ESLAFASILK DGTPIRLTGQ DSERGTFAQR NLVLHDSETG EEFVALHHLD DCAASFTVHN
     SPLSEGSVLG FEYGYNVYSP ETLVMWEAQY GDFANAAQVY FDQFISAGRA KWGQKSGLVM
     LLPHGYEGQG PEHSSGRVER FLQLAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL
     VIMTPKSLLR NPNTVSEVQE LSESRFKPVY EQSGLSHAYE KVTRVVLSSG KVSIDISDHF
     NKMEGDKDWL HIARIEQLYP FPAKDTKELF AKLPNLQEIV WVQEEPQNMG AWSYISPYLS
     EIAPKGVNVQ YIGRRRRSSP AEGDPTVHKK EQERIVSDSL TRKN
//