ID A0A089HJR9_PAEDU Unreviewed; 961 AA.
AC A0A089HJR9;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 41.
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=PDUR_01835 {ECO:0000313|EMBL:AIQ10895.1};
OS Paenibacillus durus (Paenibacillus azotofixans).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=44251 {ECO:0000313|EMBL:AIQ10895.1, ECO:0000313|Proteomes:UP000029409};
RN [1] {ECO:0000313|EMBL:AIQ10895.1, ECO:0000313|Proteomes:UP000029409}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1735 {ECO:0000313|EMBL:AIQ10895.1,
RC ECO:0000313|Proteomes:UP000029409};
RA den Bakker H.C., Tsai Y.-C., Martin N., Korlach J., Wiedmann M.;
RT "Comparative genomics of the Paenibacillus odorifer group.";
RL Submitted (AUG-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; CP009288; AIQ10895.1; -; Genomic_DNA.
DR RefSeq; WP_042204824.1; NZ_CP009288.1.
DR AlphaFoldDB; A0A089HJR9; -.
DR STRING; 44251.PDUR_01835; -.
DR KEGG; pdu:PDUR_01835; -.
DR eggNOG; COG0567; Bacteria.
DR OrthoDB; 9759785at2; -.
DR Proteomes; UP000029409; 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 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:UP000029409};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052, ECO:0000256|HAMAP-
KW Rule:MF_01169}.
FT DOMAIN 596..792
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 527..552
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 536..552
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 961 AA; 107089 MW; AEDBD02D057BE323 CRC64;
MSAKESYNES VWSKYYGPNL GYIQEKYEHF AEDPFSVEAH YRELFTIYGS PPLTSEAART
PGPALPADTD WLRKAVRASK LIASIRIFGH LAADIDPLGQ GHTSMAKWLD PETYELTRED
LLALPASLIW ENAPQDVLTG WDAYHRMRQT YTKTIAYEFS HVHDEQELRW LNSQAESATS
PAPLTPAERK GLLGRLIQVE QFETFLHKTF VGQKRFSLEG NDALVPMLDE IVRAAAHDGA
EHILMGMAHR GRLNVLAHIL GKPYDIIFSE FHHSPNKELF PSEGSMGINY GWTGDVKYHL
GADRAFHEGE TVRARLTLAN NPSHLEFVNP VVEGFARAAQ EVRSAPGLPV LDTNKAMAVL
MHGDAAFPGE GIVAETLNIG QLQGYQNGGT IHIIVNNRIG FTTESEDSRS THYASDLAKG
YEIPIVHVNA DDPEACIAAV RLASAYRNLF KKDFLIDLIG YRRHGHNEMD DPEMTQPIVY
GKVKNHPTVF RIYAERLERE KVITKDELAK MSAEADNVLQ QAYERMKEGK QKSGETKTAV
ALQTDEESSA PTAVPLGRLQ SINRQLLSFP EGFKVYPKLQ RILQRRKDLL NDGEKVDWAL
AETLAFATIL QDGTPIRLSG QDAQRGTFSQ RHLVLHDSES GELYYPLHQL EDAKASFGVY
NSPLSEASVI GYEYGYNVFA PETFVLWEAQ YGDFANAAQV IIDQFISAGR AKWTQRSNLA
ILLPHGYEGQ GPEHSSGRLE RYLQLSAEEN WTVANLTSAA QYFHLLRRQA SLGGQADARP
LVIMTPKSLL RNPRSASSGL ELASGQFQPV LPEPLLGQTP GTVTRLVVCS GKIAIDLQAE
LEAAPGQDLS WLHILRLEQL YPFPARELAV YLNAFTSLQE IVWVQEEPKN MGAWSYIEPR
LRAIAPGNTA VRYIGRPERS SPASGYADIH TFEQRRIVTE ALNLNSQTKA AVPSPSGTVS
R
//
