ID ODO2_BARVB Reviewed; 411 AA. AC Q8GCY1; DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2003, sequence version 1. DT 24-JAN-2024, entry version 87. DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; DE EC=2.3.1.61 {ECO:0000250|UniProtKB:P0AFG6}; DE AltName: Full=2-oxoglutarate dehydrogenase complex component E2; DE Short=OGDC-E2; DE AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex; GN Name=sucB; OS Bartonella vinsonii subsp. berkhoffii. OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=40933; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=12874367; DOI=10.1128/iai.71.8.4818-4822.2003; RA Gilmore R.D. Jr., Carpio A.M., Kosoy M.Y., Gage K.L.; RT "Molecular characterization of the sucB gene encoding the immunogenic RT dihydrolipoamide succinyltransferase protein of Bartonella vinsonii subsp. RT berkhoffii and Bartonella quintana."; RL Infect. Immun. 71:4818-4822(2003). 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:0000250|UniProtKB:P0AFG6}. 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:0000250|UniProtKB:P0AFG6}; CC -!- COFACTOR: CC Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088; CC Note=Binds 1 lipoyl cofactor covalently.; CC -!- PATHWAY: Amino-acid degradation; L-lysine degradation via saccharopine CC pathway; glutaryl-CoA from L-lysine: step 6/6. CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral CC symmetry. Part of the 2-oxoglutarate dehydrogenase (OGDH) complex CC composed of E1 (2-oxoglutarate dehydrogenase), E2 (dihydrolipoamide CC succinyltransferase) and E3 (dihydrolipoamide dehydrogenase); the CC complex contains multiple copies of the three enzymatic components (E1, CC E2 and E3). {ECO:0000250|UniProtKB:P0AFG6}. CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family. CC {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AY160679; AAN78227.1; -; Genomic_DNA. DR AlphaFoldDB; Q8GCY1; -. DR SMR; Q8GCY1; -. DR BRENDA; 2.3.1.61; 7855. DR UniPathway; UPA00868; UER00840. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0033512; P:L-lysine catabolic process to acetyl-CoA via saccharopine; IEA:UniProtKB-UniPathway. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR CDD; cd06849; lipoyl_domain; 1. DR Gene3D; 2.40.50.100; -; 1. DR Gene3D; 3.30.559.10; Chloramphenicol acetyltransferase-like domain; 1. DR Gene3D; 4.10.320.10; E3-binding domain; 1. DR InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS. 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; 1. 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; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS00189; LIPOYL; 1. DR PROSITE; PS51826; PSBD; 1. PE 3: Inferred from homology; KW Acyltransferase; Lipoyl; Transferase; Tricarboxylic acid cycle. FT CHAIN 1..411 FT /note="Dihydrolipoyllysine-residue succinyltransferase FT component of 2-oxoglutarate dehydrogenase complex" FT /id="PRO_0000162258" FT DOMAIN 2..77 FT /note="Lipoyl-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT DOMAIN 111..148 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170" FT REGION 82..115 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 83..113 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 382 FT /evidence="ECO:0000250|UniProtKB:P0AFG6" FT ACT_SITE 386 FT /evidence="ECO:0000250|UniProtKB:P0AFG6" FT MOD_RES 43 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" SQ SEQUENCE 411 AA; 43841 MW; 4BE837429BDE913A CRC64; MTTEIRVPTL GESVTEATVG KWFKKLGEAV AIDEPLVELE TDKVTVEVPS PVAGKLFEII AKEGDTVEVN ALLGAVEAGA ASVAKSPSSS ETSVSAAPSE LEQSSSSNTM PPAPSAAKLM AENNIAKSDI LGSGKRGQIL KEDVLNVLAQ GVKTSPPAVS ASSSTPVSVS SSAVAPVQEM REERVRMTKL RQTIARRLKD AQNTAAMLTT FNEVDMSAVM GLRKRYKDLF EKKHGVKLGF MGFFTKAVCH ALKELPAVNA EIDGTDIIYK NYVNAGIAVG TDKGLVVPVV RDADQMSLAE IEKEIGRLGR LARDGKLAVS DMQGGTFTIT NGGVYGSLMS TPILNAPQSG ILGMHAIKER AMVVDGQIAI RPMMYLALSY DHRIVDGQEA VTFLVRVKES LEDPERLVLD L //