ID C1A2J5_RHOE4 Unreviewed; 1253 AA.
AC C1A2J5;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000313|EMBL:BAH34830.1};
DE EC=1.2.4.2 {ECO:0000313|EMBL:BAH34830.1};
GN Name=sucA {ECO:0000313|EMBL:BAH34830.1};
GN Synonyms=odhA {ECO:0000313|EMBL:BAH34830.1};
GN OrderedLocusNames=RER_41220 {ECO:0000313|EMBL:BAH34830.1};
OS Rhodococcus erythropolis (strain PR4 / NBRC 100887).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus; Rhodococcus erythropolis group.
OX NCBI_TaxID=234621 {ECO:0000313|EMBL:BAH34830.1, ECO:0000313|Proteomes:UP000002204};
RN [1] {ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RA Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S.,
RA Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.;
RT "Comparison of the complete genome sequences of Rhodococcus erythropolis
RT PR4 and Rhodococcus opacus B4.";
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:BAH34830.1, ECO:0000313|Proteomes:UP000002204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PR4 / NBRC 100887 {ECO:0000313|Proteomes:UP000002204};
RX PubMed=16423019; DOI=10.1111/j.1462-2920.2005.00899.x;
RA Sekine M., Tanikawa S., Omata S., Saito M., Fujisawa T., Tsukatani N.,
RA Tajima T., Sekigawa T., Kosugi H., Matsuo Y., Nishiko R., Imamura K.,
RA Ito M., Narita H., Tago S., Fujita N., Harayama S.;
RT "Sequence analysis of three plasmids harboured in Rhodococcus erythropolis
RT strain PR4.";
RL Environ. Microbiol. 8:334-346(2006).
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; AP008957; BAH34830.1; -; Genomic_DNA.
DR RefSeq; WP_019749330.1; NC_012490.1.
DR AlphaFoldDB; C1A2J5; -.
DR GeneID; 57485984; -.
DR KEGG; rer:RER_41220; -.
DR PATRIC; fig|234621.6.peg.4660; -.
DR eggNOG; COG0508; Bacteria.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_11; -.
DR UniPathway; UPA00223; UER00997.
DR Proteomes; UP000002204; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Multifunctional enzyme {ECO:0000256|ARBA:ARBA00023268};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000313|EMBL:BAH34830.1};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 902..1098
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 24..128
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 812..839
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 40..59
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..92
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1253 AA; 137038 MW; 4249D49D2E15DF13 CRC64;
MSSSSTSQFG QNQWLVDEMY QRFQDDPSSV DPSWHEFLTD YSPDSANTGG GNGTASNGNA
AAPAAVVAPP AAPKATPPAP KTAPPAPPAK AAAPAPAKTA APAAKAAPAK PAAAKPAAAP
AKPAPAGGAE ETKVLRGAAA AVVKNMSLSL EIPTATSVRA IPAKLMFDNR IVINNHLART
RGGKISFTHL LGYAIVQAVN AFPNMNRHFA EIDGKPNAVT PEHTNLGLAI DLPGKDGNRS
LVVAAIRNTE SMNFVQFHAA YEDIVRRARE GKLTGEDFTG VTISLTNPGG IGTVHSVPRL
MKGQGAIIGA GAMEYPAEFQ GASDEKLAEM GVGKLMTLTS TYDHRIIQGA ESGDFLRTIH
NLLISDEFYD EIFHALGNPY EPVRWRKDVP EGAVDKNTRV LELIAAYRDR GHLMADTDPL
QFVKDKFHSH PDLDVISHGL TLWDLDREFK VGGFHGQEKM KLRDVLSVLR DAYCRHVGVE
YTHILETDQR QWIQDRVEGH HAKPSVAQQK YILSKLNAAE AFETFLQTKY VGQKRFSLEG
AEAVIPMMDA VIDQAAEHQL DEVVIGMPHR GRLNVLANIV GKPYSKIFTE FEGNMNPAAA
HGSGDVKYHL GASGTYIQMF GDNDIAVSLT ANPSHLEAVD PVLEGLVRAK QDILDKGEEG
FTVLPLMLHG DAAFAGQGVV AETLNLSLLR GYRTGGTVHI VVNNQVGFTT APEHSRSSEY
CTDVAKMIAA PVFHVNGDDP EACVWVAQLA VDFREKFGKD VVIDLICYRR RGHNEGDDPS
MTQPAMYDVI DTKRSVRKSY TESLIGRGDI SLKEAEDALR DYQGQLERVF NEVRELEKFQ
PEPSESVELD QTPPARLTTA VAPEVLERIG DAFVNVPDGF TVHPRVKPVA EKRREMAREG
HVDWAFAELL AFGSLAEQGA LIRLAGQDSK RGTFTQRHSV LIDRKTGNEY SPIAKIAADA
ENGGKFMVYD SALTEYAGLG FEYGYSVGNP DALVLWEAQF GDFVNGAQTI IDEFISSGEA
KWGQLSDVVL LLPHGHEGQG PDHTSGRIER FLQLCAEGSM TVAVPSTPAS YFHLLRRHHL
DGIRRPLVVF TPKSMLRNKA AVSNVEDFTT GKFRSVFEEP AFESGESARE SVKRVLLVSG
KLYWELLAKK HKDERDDIAI VRMEQLYPVP KRRLKETLDR YPNADQFRWV QEEPANQGAW
PFLGLALPDL LPETLTGIKR ISRRPMSAPS SGSSKVHAVE QQEILDEAFL PTN
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