ID A0A1B9AHU2_9BACI Unreviewed; 946 AA.
AC A0A1B9AHU2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
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 ORFNames=A8L44_11310 {ECO:0000313|EMBL:OCA83420.1};
OS Bacillus sp. FJAT-27986.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1743146 {ECO:0000313|EMBL:OCA83420.1, ECO:0000313|Proteomes:UP000092673};
RN [1] {ECO:0000313|EMBL:OCA83420.1, ECO:0000313|Proteomes:UP000092673}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-27986 {ECO:0000313|EMBL:OCA83420.1,
RC ECO:0000313|Proteomes:UP000092673};
RA Liu X., Pan Z., Shi H., Ge C., Che J., Lan J., Chen Q., Zhu Y., Wang J.,
RA Liu B., Liu G.;
RT "Bacillus sp. FJAT-27986.";
RL Submitted (MAY-2016) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OCA83420.1}.
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DR EMBL; MAYV01000016; OCA83420.1; -; Genomic_DNA.
DR RefSeq; WP_066107008.1; NZ_MAYV01000016.1.
DR AlphaFoldDB; A0A1B9AHU2; -.
DR STRING; 1743146.A8L44_11310; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000092673; 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; 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 {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:UP000092673};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 599..795
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 946 AA; 106285 MW; FE571C70F33894A0 CRC64;
MKLDTPVTNP WLEFQGPNLG YVQEMYEVFL QDPEQVDPDL VRLFEEWGPP RLEETEQTRG
NQSKEVSDGQ FTAKMMYKVS QAIKLAEDIR INGHLAADIY PLYSKVKKDI NLGLGKYDLT
TDDLKAMPAS LISDVLPANI QNGHEAIEYL KVLYTRTIAF EFDHIHDMEE KKWLTQMVEQ
TASGFAISAA KKKNLLKRLT EVDGFERFLH KTFVGQKRFS IEGVDSLVPL LDELVSRSVR
GGTNSINIGM AHRGRLNVLA HVLGKPYKKI FSEFQHAPDK KLVPSEGSIG VTFGWTGDVK
YHLGADRKIK EENTREAVIT LANNPSHLEF VNPIVNGYTR AVQDDRSQKG FPVQDSNSSM
SIIIHGDAAF PGQGIVAETL NLSRLNGYQT GGTVHIIANN MIGFTTESRD SRSTRYSSDL
AKGYEIPIIH VNADDPEAVL AAAYVAILYR QNFKKDFLID LIGYRRYGHN EMDEPMTTNP
AMYKMVHEHP TPREVYAKRL VDEGLVTEEE VARLDQEHFD MLKEYYNQVG EKEDSPLEAA
DVPKIIESGI PNVDTKVELD VLKQINAELL KRPENFKVFN KLDKILMRRQ NALEEGNKVD
WALAETLAFA TILQDGTPVR LTGQDSERGT FAHRNIVLHD SETGETYSPL HGLEGAKASF
AVHNSPLSEA AVIGFEYGYN VQSPDTLVLW EAQYGDFANT AQVLFDQFIA AGRAKWGQKS
GLVMLLPHGY EGQGPEHSSA RLERYLSLAA ENNWTVANLS SAAQYFHILR RQAAILGKEE
VRPLVLMTPK SLLRNPTVAS TAEELSDGEF KSFIEQPGLG TKKDSVERIV CCTGKMAIDL
SQAIEAQENL DWLHIVRIEE IYPFPLKGVQ ELFASYPNLK EIAWVQEEPK NMGAWNFVEP
RLRIAAPEGV KVEYIGRRRR SSPAEGDPTI HKQGQNRIIN SALTRE
//
