ID A0A1Y5KM52_9BACL Unreviewed; 967 AA.
AC A0A1Y5KM52;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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=B1748_05690 {ECO:0000313|EMBL:OUS78248.1};
OS Paenibacillus sp. MY03.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=302980 {ECO:0000313|EMBL:OUS78248.1, ECO:0000313|Proteomes:UP000195591};
RN [1] {ECO:0000313|EMBL:OUS78248.1, ECO:0000313|Proteomes:UP000195591}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MY03 {ECO:0000313|EMBL:OUS78248.1,
RC ECO:0000313|Proteomes:UP000195591};
RA Liu H., Cheng Y., Gu J.Y., Han W.J.;
RT "Draft genome of a polysaccharide-degrading bacterium Paenibacillus sp.
RT MY03.";
RL Submitted (MAR-2017) 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:OUS78248.1}.
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DR EMBL; MXQD01000004; OUS78248.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y5KM52; -.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000195591; 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; 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:UP000195591};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 606..802
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 967 AA; 107261 MW; 18FC94ABE5A2BDE7 CRC64;
MSIHDDHNSS PWKSYYGPNL GYVQEQYEQF LQDPNSVETS VREQFVLWGA PPSDTVAAQA
SASASARTSS AAVVPGPVDS NMLKKVVAAH QLMLNIRRYG HLGADINPLG ISRAADTKLL
EPETFGLTQQ DLASIPASLI WDNAPASVSN GWDAIVRLRE IYTRSAAYEF THIHDENERI
WLNKQAESGD FPAPLSKREK ETLLERLLQV EQFESFIHKT FVGQKRFSIE GVDMLVPVLD
EIVRAVAHDG AHDILIGMAH RGRLNVLTHV LGKPYEKIFS EFHHSPNKEL VPSEGSIGIN
YGWSGDVKYH LGADRAFTEG ETVRARVTLA NNPSHLEFVN PIVEGYTRAA QEDRSKPGFP
VQDQHKAVTV CVHGDAAFIG EGIVAETLNF NNLQGYRNGG TIHIIANNRL GFTTNSVDSR
STHYASDLAK GFDIPIIHVN ADDPEACLAA VRLACEYRLI YNKGFVIDLI GYRRYGHNEM
DDPDATQPLV YSKVRSHPTV ANIYAEQLKS EKTITVEQAD QLRAKTLAAL QAGYDAMKAN
EGKAHVQVTQ ESGVIVPEDV PTAVPMETLK EINLELLNRP EGFTEYSKLQ RILQRRATSL
NDGEKLDWAH AETLAFATIL ADGTPIRLSG QDSERGTFAH RHIMLNDNAT AEKFTPLHMF
PQAKASFAVH NSPLSETAVL AFEYGYNVFA PESFVIWEAQ FGDFANVAQV IFDQFMSAGR
AKWSQKSGVA VLLPHGYEGQ GPEHSSARLE RFLQLSADNN WTVANLTTSA QYFHLLRKQA
AMLGSDSVRP LILMAPKSLL RNPRVASHGV EFSEGSFKPV LPQFSFTESK AAKEKVKRLL
LGTGKVMVDL DEALSSKDEG EFGWLRVARV EQLYPLPQAE LERIIAQFPK LEEIVWVQEE
PKNQGSWSYM EPRLRELASG KAVVRYIGRP DRASTATGHQ EIHAAEQQSI ISSALNGQPF
QSSLVRG
//
