ID A0A1H1XX90_9ACTN Unreviewed; 1302 AA.
AC A0A1H1XX90;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:SDT13783.1};
GN ORFNames=SAMN04488570_3632 {ECO:0000313|EMBL:SDT13783.1};
OS Nocardioides scoriae.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=642780 {ECO:0000313|EMBL:SDT13783.1, ECO:0000313|Proteomes:UP000198859};
RN [1] {ECO:0000313|Proteomes:UP000198859}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22127 {ECO:0000313|Proteomes:UP000198859};
RA Varghese N., Submissions S.;
RL Submitted (OCT-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; LT629757; SDT13783.1; -; Genomic_DNA.
DR STRING; 642780.SAMN04488570_3632; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000198859; Chromosome i.
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 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 Coiled coil {ECO:0000256|SAM:Coils};
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 953..1146
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 43..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1269..1302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 863..890
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 47..61
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..166
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 167..181
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1277..1302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1302 AA; 143852 MW; 79BBBB04A46EC604 CRC64;
MPESTEESSP SGFGANEWLV DEMYERFQRD PHSVDQVWWD FFGKDARNGS SGSTAAGTSQ
AGDRAADQAP DRAPAADAPA SPGASNGHAH IVESTGAPKR RPQASRPAPS TPTRPSTTSP
THDPKQAEQL SEQKFSSTST PAKEGSGQGT TSKAATTSSG SRSTGRAEAD RSPEEAVSDE
PRYTVLRGAP ARTVANMDAS LSVPTATSVR TVPVKLLWDN RIVINNHLAR ARGGKVSFTH
LIGYALVKAL RSMPEMNVGF DVVDGKPNLI TPAHINLGLA IDLPKPDGTR QLLVPSIKAA
ETMDFAQFWT AYEELVRKAR NGKLAVTDFQ GTSISLTNPG TIGTNHSVPR LMKGQGAILG
VGSMEYPAAF QGASEETLTR NAISKIMTLT STYDHRVIQG AQSGEFLRRI HQLLLGEEGF
YDEIFRALRI PYEPIRWSND ISANHDDEIS KQARILELIH AYRVRGHMMA DTDPLEYKQR
SHPDLEVESH GLTLWDLDRE FATGSFGGER RFMKMRSILG ILRDSYCRTV GIEYMHIQDP
EQRRWIQERV EQPHRKPPRE EQLRILLKLN QAEAFETFLQ TKFVGQKRFS LEGGETTVPL
IDEICEASAE AGLDEVTIGM AHRGRLNVLA NIVGKSYSQI FREFEGNIDP RTVQGSGDVK
YHLGAEGEFV SDNGDKVKVS VAANPSHLEA VDPVLEGIAR AKQDVLNQGE AFPVLPLLVH
GDAAFAGQGV VAETLNLSQL RGYRTGGTVH VVVNNQVGFT TSPAASRSSL YCTDVARMVQ
APIFHVNGDD PEACIRVARL AFEYRQAFNK DVVIDLVCYR RRGHNEGDDP SYTQPLMYDL
IEQKRSVRKL YTESLIGRGD ITLEEAEQVL KDYQQQLERV FTEVREATST PDSWTTVPDY
PEKSHEEYTT AISPEALKRI SDSYVSAPEG FTVHPKVLPQ LQKRSAAMTD GPIDWGAGEI
LAFGSLLMDG RPVRLSGQDS RRGTFASRFA TIIDRKNAHE WTPLSNLTED QASFFVYDSL
LSEYAALGFE YGYSVARPDA LVAWEAQFGD FVNGAQTVID EFITSGETKW GQQSGVVLLL
PHGYEGQGPD HSSARIERFL TMGADDAFVV AQPSTPASYF HLLRRHALGD RHRPMVVFTP
KSMLRRKEAA SRPEDFTSGT FQPLVPDTQV DPEKVHTLVL CSGRITWDLM VHREKTQGDA
KTTAIARLEQ LYPRPEQELL AEVAKYPNLR AVRWVQDEPA NMGPAPHLRL NLFPLLDLPV
EVVSRAASSS PAVGQAKRHT EENKTLMSAA FEEPRGLAEE KY
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