ID A0A1N6J9Y7_9RHOB Unreviewed; 512 AA.
AC A0A1N6J9Y7;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex {ECO:0000256|ARBA:ARBA00019511, ECO:0000256|RuleBase:RU361138};
DE EC=2.3.1.61 {ECO:0000256|ARBA:ARBA00012945, ECO:0000256|RuleBase:RU361138};
DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2 {ECO:0000256|RuleBase:RU361138};
GN ORFNames=SAMN05444722_1972 {ECO:0000313|EMBL:SIO41174.1};
OS Rhodovulum sp. ES.010.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Rhodovulum.
OX NCBI_TaxID=1882821 {ECO:0000313|EMBL:SIO41174.1, ECO:0000313|Proteomes:UP000184943};
RN [1] {ECO:0000313|EMBL:SIO41174.1, ECO:0000313|Proteomes:UP000184943}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ES.010 {ECO:0000313|EMBL:SIO41174.1,
RC ECO:0000313|Proteomes:UP000184943};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: E2 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC complex which catalyzes the second step in the conversion of 2-
CC oxoglutarate to succinyl-CoA and CO(2). {ECO:0000256|ARBA:ARBA00004052,
CC ECO:0000256|RuleBase:RU361138}.
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 ECO:0000256|RuleBase:RU361138};
CC -!- COFACTOR:
CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC Evidence={ECO:0000256|ARBA:ARBA00001938};
CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine
CC pathway; glutaryl-CoA from L-lysine: step 6/6.
CC {ECO:0000256|ARBA:ARBA00005145, ECO:0000256|RuleBase:RU361138}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000256|ARBA:ARBA00007317, ECO:0000256|RuleBase:RU361138}.
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DR EMBL; FSRS01000001; SIO41174.1; -; Genomic_DNA.
DR RefSeq; WP_074219927.1; NZ_FSRS01000001.1.
DR AlphaFoldDB; A0A1N6J9Y7; -.
DR STRING; 1882821.SAMN05444722_1972; -.
DR OrthoDB; 9805770at2; -.
DR UniPathway; UPA00868; UER00840.
DR Proteomes; UP000184943; Unassembled WGS sequence.
DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniRule.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniRule.
DR CDD; cd06849; lipoyl_domain; 2.
DR Gene3D; 2.40.50.100; -; 2.
DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1.
DR Gene3D; 4.10.320.10; E3-binding domain; 1.
DR InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR023213; CAT-like_dom_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR006255; SucB.
DR NCBIfam; TIGR01347; sucB; 1.
DR PANTHER; PTHR43416:SF5; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43416; DIHYDROLIPOYLLYSINE-RESIDUE SUCCINYLTRANSFERASE COMPONENT OF 2-OXOGLUTARATE DEHYDROGENASE COMPLEX, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF00198; 2-oxoacid_dh; 1.
DR Pfam; PF00364; Biotin_lipoyl; 2.
DR Pfam; PF02817; E3_binding; 1.
DR SUPFAM; SSF52777; CoA-dependent acyltransferases; 1.
DR SUPFAM; SSF47005; Peripheral subunit-binding domain of 2-oxo acid dehydrogenase complex; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 2.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 2.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|RuleBase:RU361138}; Lipoyl {ECO:0000256|RuleBase:RU361138};
KW Reference proteome {ECO:0000313|Proteomes:UP000184943};
KW Transferase {ECO:0000256|RuleBase:RU361138};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532,
KW ECO:0000256|RuleBase:RU361138}.
FT DOMAIN 2..77
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 112..187
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT DOMAIN 212..249
FT /note="Peripheral subunit-binding (PSBD)"
FT /evidence="ECO:0000259|PROSITE:PS51826"
FT REGION 81..109
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 187..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..239
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 512 AA; 54285 MW; 076C9B43E3686FBD CRC64;
MSTEVRVPTL GESVTEATVA TWFKQPGDAV SADEMLCELE TDKVTVEVPA PAAGTLSEIV
AGEGETVSVD ALLATISEGA GKPAEGKKKA KAPADEGRSV PEEAASEGEG EKIDVMVPSL
GESVTEATVS TWFKQAGDPV ARDEMLCELE TDKVSVEVPA PASGTLSEIL AREGETVEAG
GKLAVMTSGK GAAPEPPAEP AAAPAGGGKD VEHAPSAKKL MAEKGLSEDD VKGTGRDGRI
MKEDVQKAAE APKPAEKPAE APKPAPAPDA ARAPIPAEDA EREERVKMTR LRQTIARRLK
DAQNTAAMLT TYNEVDMSGV MALRKEYKDL FEKKHGVKLG FMSFFTKACC HALTEVPEVN
AEIDGTDIVY KKFVHMGIAV GTPNGLVVPV LRNADTMSFA EIEKRIAELG IRARDGKLSM
AEMQGGTFTI SNGGVYGSLM SSPILNPPQS GILGMHKIQD RPMVVGGQIV IRPMMYLALS
YDHRIVDGKG AVTFLVRVKE ALEDPRRLLM DL
//
