ID ODO1_BACP2 Reviewed; 944 AA.
AC A8FE66;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 94.
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=BPUM_1862;
OS Bacillus pumilus (strain SAFR-032).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=315750;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SAFR-032;
RX PubMed=17895969; DOI=10.1371/journal.pone.0000928;
RA Gioia J., Yerrapragada S., Qin X., Jiang H., Igboeli O.C., Muzny D.,
RA Dugan-Rocha S., Ding Y., Hawes A., Liu W., Perez L., Kovar C., Dinh H.,
RA Lee S., Nazareth L., Blyth P., Holder M., Buhay C., Tirumalai M.R., Liu Y.,
RA Dasgupta I., Bokhetache L., Fujita M., Karouia F., Eswara Moorthy P.,
RA Siefert J., Uzman A., Buzumbo P., Verma A., Zwiya H., McWilliams B.D.,
RA Olowu A., Clinkenbeard K.D., Newcombe D., Golebiewski L., Petrosino J.F.,
RA Nicholson W.L., Fox G.E., Venkateswaran K., Highlander S.K.,
RA Weinstock G.M.;
RT "Paradoxical DNA repair and peroxide resistance gene conservation in
RT Bacillus pumilus SAFR-032.";
RL PLoS ONE 2:E928-E928(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; CP000813; ABV62533.1; -; Genomic_DNA.
DR RefSeq; WP_012010256.1; NZ_VEIS01000001.1.
DR AlphaFoldDB; A8FE66; -.
DR SMR; A8FE66; -.
DR STRING; 315750.BPUM_1862; -.
DR KEGG; bpu:BPUM_1862; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000001355; 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 Gene3D; 1.10.287.1150; TPP helical domain; 1.
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; 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; 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; 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_1000065697"
FT REGION 918..944
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 944 AA; 106822 MW; 5CF1400B2F45876F CRC64;
MFQNDVKQPL SWEEFHGPNL GYVLELYDQY VQDPTSVDED LRGIFDELGA PPSEMKEEIG
KKENSVVTSE QIQKIASVVK LAEDIRTYGH LNASVNPLRK EKELQELFPL KEYGLTEEDV
KNIPISIISP DAPKHISNGI EAINHLRNTY KRTISFEFDH VHDFEERNWL SKSIESGELF
KKKPADKLVS VFKRLTEVEQ FEQFLHKTFV GQKRFSIEGL DALVPVLDEI ISESVTQGTS
NINIGMAHRG RLNVLAHVLG KPYEIIFSEF QHAPNKELVP SEGSIGISYG WTGDVKYHLG
ADRQIKDEDT KSARVTLANN PSHLEFIDPI IEGSTRAAQE LRTQKGYPAQ DVEKALAILI
HGDAAFPGEG IVAETLNLSQ LVGYQVGGTI HIIANNMIGF TTESNESRST KYASDLAKGF
EIPIVHVNAD DPEACLAAVQ LAVEYRKRFK KDFLIDLIGY RRYGHNEMDE PSTTQPMLYD
AVRKHKTVKN IFADKLVSEG LLTKEQREEI EQAVATRIEE AYQKVPSKKE HTIQEIELPE
PVSNGFPAVD TSVEFDVLRK LNEELISWPD DFQVFGKLKR ILEKRAKVFT DDRKVEWSLG
EALAFASILK DGTPIRMTGQ DSERGTFAQR NLVLHDSQTG NEFIALHELS DANASFTVHN
SPLSEGSVIG FEYGYNVYSP ETLVIWEAQF GDFANAAQVY FDQFISAGRA KWGQKSGLVM
LLPHGYEGQG PEHSSGRTER FLQSAAENNW TVANLTSAAQ YFHILRRQAK MLLREEIRPL
VIMTPKSLLR NPNSLSEVQE LTDGQFQPVL EQPGLVHDHE KVSRLVLSSG KVSIDISDRF
TQMEEPKDWL HIARVEQLYP FPAKDIKAIL SKLTNLEEIV WTQEEPQNMG AWGYIEPYLR
EIAPEKVKVR YIGRRRRSST AEGDPTVHKK EQERIVSDSL TRKN
//
