ID A0A1C6TCL9_9ACTN Unreviewed; 1241 AA.
AC A0A1C6TCL9;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:SCL39560.1};
GN ORFNames=GA0070624_6609 {ECO:0000313|EMBL:SCL39560.1};
OS Micromonospora rhizosphaerae.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=568872 {ECO:0000313|EMBL:SCL39560.1, ECO:0000313|Proteomes:UP000199413};
RN [1] {ECO:0000313|Proteomes:UP000199413}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 45431 {ECO:0000313|Proteomes:UP000199413};
RA Varghese N., Submissions Spin;
RL Submitted (JUN-2016) 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; FMHV01000002; SCL39560.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C6TCL9; -.
DR STRING; 568872.GA0070624_6609; -.
DR OrthoDB; 9759785at2; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000199413; Unassembled WGS sequence.
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 Reference proteome {ECO:0000313|Proteomes:UP000199413};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 898..1093
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 46..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 833..853
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1241 AA; 137061 MW; 29C0FF1FBC89268E CRC64;
MSTQQTSQEN PLAGFGPNEW IVEEMYQRYL ADPSSVDSAW HDFFADYRPA PGAATPRPAE
PKAQPAARPE PAGQQEPAAA VAQQPAAAKP APAKPAPAKP AAAKPAPAAK AAPTKPAVKA
PAPAGASTTP LRGVAAKIVQ NMDASLSVPT ATSVRSVPAK LLVDNRIVIN NHLARGRGGK
VSFTHLIGYA MVRALVEHPE MNNSFAEVDG KPAVVRPEHV NLGIAIDLTK PDGSRNLVVP
SIKACEQMDF RQFWQAYEDV VRRARRNELT MEDYAGTTIS LTNPGGIGTV HSIPRLMQGQ
SAIIGVGAME YPAPYQGMSE ATLAELAVSK VITLTSTYDH RIIQGAQSGE FLKVMHELLL
GERGFYDDVF TSLRIPYEPV RWMRDVAVDS EGQINKTARV HELIHAYRVR GHLMADTDPL
EFKIRRHPDL DVLQHGLTLW DLDRVFPVNG FAGRQRMKLR EILGVLRDSY CRRVGIEYMH
IQDPEERRWL QERVERKYEK PTADEQKHVL NRLNAAEAFE TFLQTKYVGQ KRFSLEGGES
LIPLLGEVLE SSAEGGLDEV VIGMAHRGRL NVLANIVGKP YEKIFSEFEG HLDPRSTQGS
GDVKYHLGQN GKFTTPDGQH AVKVSVVANP SHLEAVDPVL EGIVRAKQDR IDLKLEGYTV
LPLAVHGDAA FAGQGVVAET LNLSQLRGYR TGGTVHVVVN NQVGFTTAPE YSRSSLYSTD
VARMIQAPIF HVNGDDPEAV VRVARLSFEY RQAFNKDVVI DMVCYRRRGH NEGDDPSMSN
PQMYRIIDSK RSVRKLYTEE LIGRGDITVE DAEELLRDYQ AQLERVFKAT RDAASTPRHL
SRSPRLVEPE PQVETATDAA VVKAIGEAHV NLPEGFTPHK RIQQLLDRRA KMSVEGNIDW
GFGEIIAFGA LLHDGVTVRL AGQDSRRGTF VQRHASVVDA KTGDDYLPLK SLTGDGERSR
FFVHDSLLSE YAAMGFEYGY SVENVNALVC WEAQFGDFVN GAQSVIDEFI SSGEVKWGQR
SAVTLLLPHG HEGQGPDHTS GRPERFLQLC AEDNMRVAIP TTPANYFHLL RRQALSPKRK
PLVVFTPKSL LRHKLCVSPV EDFTTGTFQP VLRDTGAPAP EQVKRVLLCS GKVYYDLFQA
RAERGVTDTA IIRMEQLYPL PVEEIRAALA LYPNAEDFAW VQEEPANQGA WSFVALNLLE
HLSEIRLRRI SRPAAAAPSV GSAKMHDVEQ AALIEAALPR P
//
