ID A0A0A1MVK2_9BACI Unreviewed; 956 AA.
AC A0A0A1MVK2;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ECO:0000313|EMBL:CEI83477.1};
GN ORFNames=BN997_03392 {ECO:0000313|EMBL:CEI83477.1};
OS Oceanobacillus oncorhynchi.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Oceanobacillus.
OX NCBI_TaxID=545501 {ECO:0000313|EMBL:CEI83477.1, ECO:0000313|Proteomes:UP000040453};
RN [1] {ECO:0000313|EMBL:CEI83477.1, ECO:0000313|Proteomes:UP000040453}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Oc5 {ECO:0000313|EMBL:CEI83477.1,
RC ECO:0000313|Proteomes:UP000040453};
RA Urmite Genomes Urmite Genomes;
RL Submitted (NOV-2014) 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; CDGG01000001; CEI83477.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A1MVK2; -.
DR STRING; 545501.BN997_03392; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000040453; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000040453};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 603..799
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 956 AA; 108198 MW; 646D61A57FAD93ED CRC64;
MPGNEESAEK FWGQFHGPNA GYLEQQYELY KEDPEQVESS IKALFDAYGA PAWMTGAEVV
FPISEQTASN GNISEDFDVT KLTSAIKLVE AIRRYGHTDA DIYSVGGYKS APSVMLDLKH
YNLTEEDLKK IPASWIWERE KEDVQTGLDV INLLKKYYTG TITFEYDHVN NDEERTWLFD
LIEEGNARFD PDQEDRKDIL KRLYEVEGFE KFLHKTFVGQ KRFSIEGLES MVPMIDYLVK
YANEDNIEHV MMGMAHRGRL AVLANVLKKP YDKIFSEFNY TRDKELMPSE GSKAINYGWT
GDVKYHFGAE KEVIHGSKVN TKITLAHNPS HLEFVNPVVE GFARAAQDER DVSGYPVRDT
NKAMPLIIHG DAAFIGEGVV AETLNLSGLP GYTTGGTVHL IANNQLGYTT DRVDGRSTRY
ASDLAKGFEI PIIRVSADDP ISCISAVKIA CEYRKKFHKD VLIDLVGYRR YGHNEMDEPR
TTQPQLYSEI DNHPSVSTLF ARAMEERNLL ESGGFDEIKN EIDTKLSDIY KGMTETEIGE
PQPKSMPEVL SNRLDQFETA VDLETLKGIN KELLKRPEGF EGFKKTERIL KRREDALEEG
NKADWGTGEA LAFASILKDG TPIRLTGQDT ERGTFAHRHV VLHDVNTGEK YSPMHGLSDV
KASFDVRNSP LSETGVLGFE YGYSVYSPST LVIWEAQFGD FANAGQVIID QFIASARAKW
DEKSNMVLLL PHGYEGQGPE HSSARLERYL QMAAENNWIV ANVTSSAQLF HLLRRQAAMR
SRPEARPLIL MTPKSSLIRD YKMASSAEEF TTGGFKTLRE QPYFDTDPKK ATRLLLGSGK
IMIDIEGEME EAEANCDWIR ALRVEQIYPF PKKAIQEEIQ KLPNLKEIVW VQEEPKNMGS
WDFVDDYLRE LLEEDQELHV ISRPKRAAPA GGIPTVHKTA HQYIIDQALN EFEGGK
//
