ID A0A1I7F4A9_9BACL Unreviewed; 974 AA.
AC A0A1I7F4A9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05421543_10154 {ECO:0000313|EMBL:SFU30983.1};
OS Alicyclobacillus macrosporangiidus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Alicyclobacillaceae;
OC Alicyclobacillus.
OX NCBI_TaxID=392015 {ECO:0000313|EMBL:SFU30983.1, ECO:0000313|Proteomes:UP000183508};
RN [1] {ECO:0000313|Proteomes:UP000183508}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17980 {ECO:0000313|Proteomes:UP000183508};
RA Varghese N.;
RL Submitted (OCT-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}.
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DR EMBL; FPBV01000001; SFU30983.1; -; Genomic_DNA.
DR RefSeq; WP_074949181.1; NZ_FPBV01000001.1.
DR AlphaFoldDB; A0A1I7F4A9; -.
DR STRING; 392015.SAMN05421543_10154; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000183508; 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 Gene3D; 1.10.287.1150; TPP helical 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:UP000183508};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 617..812
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 62..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 974 AA; 107658 MW; C21313F82D587B71 CRC64;
MATRRNRPAP ASWQALYGPN LGWALELYER YQAHPQSVDD QTRALFERLG PPPAEVLAGR
AADADTDGLA SDKAAQGRAG DAAWQAQPGT AAAVDTQRIV AAQRLARNIR MYGHLEARIN
PIGEPPAPAA ILDLQNYGLT EEDLARIPAH WVWAHAPADV RDAKTALQRL RRVYTGSLAY
EFAHVHDPEE HAWLTRHVES SEWPRPLPAE QAKALLRRLI EVDEFEKFLH RTFVGQKRFS
IEGVDMLVPM LDRLIYLTVQ SGARDVMIGM AHRGRLNVLA HVLGKPYQAI FSEFHAAPNK
ELVPSEGSMG INYGWTGDVK YHLGASRDVG DGHEVQARLR LANNPSHLEF VNPVVEGFAR
AAQDDRGQAG APGHDMDAAV AVLVHGDAAF PGEGIVAETL NLSRLPGYTT GGTIHIIANN
QLGFTAVPEE GRSTRYASDL AKGFEIPIVH VNADDPEACL AAIELAHAYR QAFHKDFLID
LVGYRRWGHN EGDDPVMTQP RMYDVIAHHP TVRELYAKRL LEAGMVQPDE VAELERQVRD
RLRQAYSQVG EEKDEAEPTW KHAGPMQSVQ AQPVPREQLQ ALNEALLARP EGFTVYPKLD
RILQRRRTAF TEPDGRVDWA HAEALAFASV LAEGIPVRLT GQDSERGTFS QRHLVLHDHR
TGQTYTPLQH LPQARASFAV HNSPLTEAAV IGFEYGYNVQ APQTLVLWEA QFGDFANAGQ
VLIDQFLSAG LAKWGQPSGL VLLLPHGYEG QGPEHSSARL ERYLQLSAEH NWRVVYPTTA
AQYFHLLRDQ AARLTVDPRP LVVMTPKSLL RNPRAASTVD ELTQGGFQPL WTEPPRPGAD
AAAVRRLILC TGKVGVDLAA ALEQAGHPEW LAVARVEQLY PFPADAVRQW AASFPGAAEL
VWLQEEPQNM GAWGYVQPHL AELFPDLPIR YVGRPARSSP AEGLADAHEQ MQRQIIAQAV
SEQGLSVHAG RESR
//
