ODO1_BACVZ
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 03-AUG-2022, entry version 92.
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}; OrderedLocusNames=RBAM_019130;
OS Bacillus velezensis (strain DSM 23117 / BGSC 10A6 / LMG 26770 / FZB42)
OS (Bacillus amyloliquefaciens subsp. plantarum).
OC Bacteria; Firmicutes; 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=(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; CP000560; ABS74275.1; -; Genomic_DNA.
DR RefSeq; WP_012117750.1; NC_009725.2.
DR AlphaFoldDB; A7Z5J9; -.
DR SMR; A7Z5J9; -.
DR STRING; 326423.RBAM_019130; -.
DR EnsemblBacteria; ABS74275; ABS74275; RBAM_019130.
DR KEGG; bay:RBAM_019130; -.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OMA; RDSYCRT; -.
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 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; 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
