ID D6XUR3_BACIE Unreviewed; 953 AA.
AC D6XUR3;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|HAMAP-Rule:MF_01169};
DE EC=1.2.4.2 {ECO:0000256|HAMAP-Rule:MF_01169};
DE AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01169};
GN Name=odhA {ECO:0000256|HAMAP-Rule:MF_01169};
GN OrderedLocusNames=Bsel_2045 {ECO:0000313|EMBL:ADH99549.1};
OS Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Salisediminibacterium.
OX NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH99549.1, ECO:0000313|Proteomes:UP000000271};
RN [1] {ECO:0000313|EMBL:ADH99549.1, ECO:0000313|Proteomes:UP000000271}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC {ECO:0000313|Proteomes:UP000000271};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Stolz J.;
RT "Complete sequence of Bacillus selenitireducens MLS10.";
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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:0000256|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:0000256|HAMAP-Rule:MF_01169};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964,
CC ECO:0000256|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:0000256|HAMAP-
CC Rule:MF_01169}.
CC -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC {ECO:0000256|HAMAP-Rule:MF_01169}.
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DR EMBL; CP001791; ADH99549.1; -; Genomic_DNA.
DR RefSeq; WP_013172971.1; NC_014219.1.
DR AlphaFoldDB; D6XUR3; -.
DR STRING; 439292.Bsel_2045; -.
DR KEGG; bse:Bsel_2045; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_9; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000000271; 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; 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 {ECO:0000256|ARBA:ARBA00023152, ECO:0000256|HAMAP-
KW Rule:MF_01169};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_01169};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 595..791
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 912..953
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..936
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 953 AA; 107618 MW; 8FB92025DC2796E3 CRC64;
MAAHDIQVRK GWQQFNGVNL GYMFEQYERY EEDPSQVDDK LRAFFDKWGA YSESGSQDNG
ERLNDSVNLK KREHVAVQAS FLAESIRRNG HLIADIMPFD TERRPEGLFN LEDFDLTKQD
LQHLSAELLS PHYSKGLQNG DDAINHLKDA YTGNIAFQFK HIQEIKERKW LFREVETGAY
KINLSDSDKT DLLQRLNKVE GFEHFLDKTF KGQKRFSVEG LDTMVPMLDQ LVKDAVNAGS
KHIFIGMAHR GRLNVLAHVL GKPYELIFSE FHDAPNPELV PSEGSTGINY GWTGDVKYHL
GADREIKESA SEATITLANN PSHLEFVNPV IEGLTRAAQD DRSKSGFPSH DPDLALPVLI
HGDAAFPGQG VVAETINLSG LRGYSTGGTI HLIANNLLGF TTDSHDSRST TYASDMARGF
DVPVIHVNAD DPESSLSAMN LAWKYRKAFG KDVVIDLIGY RRYGHNEMDE PLATQPSLYK
IIQKHPTVFE LYGEKLRQES KVTDEQLRKM RKEFTDKLNQ QFDKIKGNKR ETIDGDMSPP
DVVTSSLERY QKNISPDSLE KVNEELLAFP ESFSVFPKLK RILERRRDAF RDGAIDWGHA
EALAFATIIK DGIPIRLTGQ DSERGTFSHR HLILHDYETG DTFSPMHYLS NANASFALHN
SPLSETACLG FEYGYNVEAP ETLTIWEAQY GDFANGAQVI LDQFISSGRA KWSQKSGLVL
LLPHGYEGQG PEHSSARLER FLTLAAENNW HVANVTKASQ YYHLLRRQAH SLGTDYVRPL
ILMAPKSLIR NERVVSSAKE MTEDEFKPVL VSPDMKASNQ VERVILTQGK IGVELETAIA
GLDEQPDWLI HVRIEELYPF PSASLRDVLQ ACGNVKEVIW LQEEPQNMGA WTYVMPYLQG
LFGAEKISFT GRRRRSSPAE GDPKVHKLEH ERMINSVLDR SSNLKGDSHN DRD
//
