ID E8NBK9_MICTS Unreviewed; 1225 AA.
AC E8NBK9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE SubName: Full=2-oxoglutarate dehydrogenase complex, dehydrogenase (E1) component {ECO:0000313|EMBL:BAJ73469.1};
GN Name=kgd {ECO:0000313|EMBL:BAJ73469.1};
GN OrderedLocusNames=MTES_0505 {ECO:0000313|EMBL:BAJ73469.1};
OS Microbacterium testaceum (strain StLB037).
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Microbacterium.
OX NCBI_TaxID=979556 {ECO:0000313|EMBL:BAJ73469.1, ECO:0000313|Proteomes:UP000008975};
RN [1] {ECO:0000313|EMBL:BAJ73469.1, ECO:0000313|Proteomes:UP000008975}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StLB037 {ECO:0000313|EMBL:BAJ73469.1,
RC ECO:0000313|Proteomes:UP000008975};
RX PubMed=21357489; DOI=10.1128/JB.00180-11;
RA Morohoshi T., Wang W.-Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037, an N-acylhomoserine
RT lactone-degrading bacterium isolated from potato leaves.";
RL J. Bacteriol. 193:2072-2073(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=StLB037;
RA Morohoshi T., Wang W.Z., Someya N., Ikeda T.;
RT "Genome sequence of Microbacterium testaceum StLB037.";
RL Submitted (FEB-2011) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00043700};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(6)-[(R)-dihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase
CC complex component E2] + succinyl-CoA = CoA + N(6)-[(R)-S(8)-
CC succinyldihydrolipoyl]-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC component E2]; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581, Rhea:RHEA-
CC COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292, ChEBI:CHEBI:83100,
CC ChEBI:CHEBI:83120; EC=2.3.1.61;
CC Evidence={ECO:0000256|ARBA:ARBA00043693};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; succinyl-
CC CoA from 2-oxoglutarate (dehydrogenase route): step 1/1.
CC {ECO:0000256|ARBA:ARBA00004813}.
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DR EMBL; AP012052; BAJ73469.1; -; Genomic_DNA.
DR AlphaFoldDB; E8NBK9; -.
DR STRING; 979556.MTES_0505; -.
DR KEGG; mts:MTES_0505; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000008975; Chromosome.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
DR CDD; cd02016; TPP_E1_OGDC_like; 1.
DR Gene3D; 3.40.50.12470; -; 1.
DR Gene3D; 3.40.50.970; -; 1.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 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 InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR032106; 2-oxogl_dehyd_N.
DR InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR InterPro; IPR023213; CAT-like_dom_sf.
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; PF00198; 2-oxoacid_dh; 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; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE 4: Predicted;
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 887..1080
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 55..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1225 AA; 134838 MW; 970722DCF7AC9AA2 CRC64;
MSSQVTGVGT SNEGEFGANE WLVDELYEQF KVDKHSVDKA WWPILEAYHP VVDESAAAGS
PPSAPAAEPK PVTAPIPVVG QTPVARTTTK PAKPQPIPAQ APTAAPSAGS ESTEEDRVTV
LKGMPKALAS NMDDSLTVPT ATSVRTIPAK LMIDNRIVIN NHMSRTRGGK VSFTHLIGWA
LIQALKEFPS QNVYYAEIDG KPSVVAPAHI NLGIAIDMPK PDGSRALLVP SIKRADTLTF
GEFLASYEDL VRRARNNKLT PADFQGTTIS LTNPGGIGTV HSVPRLMRGQ GAIIGAGALD
YPAEFQGSSA KTLNELAIGK TITLTSTYDH RVIQGAGSGE FLKKVHELLI GQRGFYDDIF
AALRIPYAPI HWAADINVDV SERIDKSARV QELINSYRVR GHLMADIDPL EYVQRTHPDL
EIESHGLTFW DLDREFVTGG LGDRRVAKLR DILGVLRDSY CRTIGVEYMH IQDPIQRKWF
QSNVEVKYIK PGHDEQLRIL SKLNQAEAFE TFLQTKYVGQ KRFSLEGGES LIPLLDQILQ
GAASKGLDGA AIGMAHRGRL NVLTNIGGKT YGQVFREFEG AVAIGSKRGS GDVKYHLGTE
GTFVGDNGEE LPVYLAANPS HLETVDGVLE GIVRAKQDRK PIGSFSWLPI LVHGDAAFAG
QGVVVETLQM SQLRGYRTGG TIHVVVNNQV GFTTTPTDAR TSVYATDVAK TIQAPVLHVN
GDDPEAVVRA AELAFLYREE FHRDVVIDLV CYRRRGHNEG DDPSMTQPLM TNLIEAKRSV
RRLYTEALVG RGDITEDEYE QAKQDFQNRL EVAFADTHEA ETGTNPVVST EAADEVPTGA
PETTGVSREV VHHIGDAFVN KPDGFTVHNK LQQLLEKRFD MSRNGGIDWA FGELLAFGSV
LMEGTPVRLA GQDSRRGTFV QRHSVLHDRK NGQEWLPLAN LSENQGRFWV YDSLLSEYAA
MAFEYGYSVE RSDALVLWEA QFGDFANGAQ SVIDEFISSA DQKWAQQSSV VLLLPHGYEG
QGPDHSSARI ERYLQMCAQD NMIVARPSTP ASYFHLLRRQ AYQRPRRPLI VFTPKAMLRL
RGATSPVEDF LEGRFEPVLD DDRGLDAGAV TRVLLHAGKI HWDLRAELDK NPNPEIALVR
LEQYYPAPID ELNRVLATYP NAELVWVQDE PENQGAWPFI ALEVDDKLGR PIRVISRAAA
ASTATGSPKV HANEHAEIMK AALAR
//
