ID ODO2_AZOVI Reviewed; 399 AA. AC P20708; Q44474; DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 134. 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; Synonyms=odhB; OS Azotobacter vinelandii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / RC NBRC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16; RX PubMed=2404760; DOI=10.1111/j.1432-1033.1990.tb15300.x; RA Westphal A.H., de Kok A.; RT "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 2. RT Molecular cloning and sequence analysis of the gene encoding the RT succinyltransferase component."; RL Eur. J. Biochem. 187:235-239(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 354-399. RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / RC NBRC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16; RX PubMed=2832161; DOI=10.1111/j.1432-1033.1988.tb13887.x; RA Westphal A.H., de Kok A.; RT "Lipoamide dehydrogenase from Azotobacter vinelandii. Molecular cloning, RT organization and sequence analysis of the gene."; RL Eur. J. Biochem. 172:299-305(1988). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-30. RC STRAIN=ATCC 478 / DSM 2289 / BCRC 14361 / JCM 21475 / KCTC 12137 / RC NBRC 102612 / NCIMB 12096 / NRRL B-14641 / VKM B-1617 / NRS 16; RX PubMed=2404759; DOI=10.1111/j.1432-1033.1990.tb15299.x; RA Schulze E., Westphal A.H., Hanemaaijer R., de Kok A.; RT "The 2-oxoglutarate dehydrogenase complex from Azotobacter vinelandii. 1. RT Molecular cloning and sequence analysis of the gene encoding the 2- RT oxoglutarate dehydrogenase component."; RL Eur. J. Biochem. 187:229-234(1990). RN [4] RP STRUCTURE BY NMR OF 1-80. RX PubMed=8529634; DOI=10.1111/j.1432-1033.1995.148_c.x; RA Berg A., Smits O., de Kok A., Vervoort J.; RT "Sequential 1H and 15N nuclear magnetic resonance assignments and secondary RT structure of the lipoyl domain of the 2-oxoglutarate dehydrogenase complex RT from Azotobacter vinelandii. Evidence for high structural similarity with RT the lipoyl domain of the pyruvate dehydrogenase complex."; RL Eur. J. Biochem. 234:148-159(1995). RN [5] RP STRUCTURE BY NMR OF 1-78. RX PubMed=8780784; DOI=10.1006/jmbi.1996.0474; RA Berg A., Vervoort J., de Kok A.; RT "Solution structure of the lipoyl domain of the 2-oxoglutarate RT dehydrogenase complex from Azotobacter vinelandii."; RL J. Mol. Biol. 261:432-442(1996). 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; M37307; AAA22138.1; ALT_SEQ; Genomic_DNA. DR EMBL; X52432; CAA36678.1; -; Genomic_DNA. DR EMBL; X52433; CAA36681.1; -; Genomic_DNA. DR PIR; S07779; S07779. DR PDB; 1GHJ; NMR; -; A=2-80. DR PDB; 1GHK; NMR; -; A=2-80. DR PDBsum; 1GHJ; -. DR PDBsum; 1GHK; -. DR AlphaFoldDB; P20708; -. DR SMR; P20708; -. DR BRENDA; 2.3.1.61; 49. DR SABIO-RK; P20708; -. DR UniPathway; UPA00868; UER00840. DR EvolutionaryTrace; P20708; -. 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 1: Evidence at protein level; KW 3D-structure; Acyltransferase; Lipoyl; Transferase; KW Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT CHAIN 2..399 FT /note="Dihydrolipoyllysine-residue succinyltransferase FT component of 2-oxoglutarate dehydrogenase complex" FT /id="PRO_0000162255" FT DOMAIN 2..77 FT /note="Lipoyl-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT DOMAIN 104..141 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170" FT ACT_SITE 370 FT /evidence="ECO:0000250|UniProtKB:P0AFG6" FT ACT_SITE 374 FT /evidence="ECO:0000250|UniProtKB:P0AFG6" FT MOD_RES 43 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT STRAND 3..6 FT /evidence="ECO:0007829|PDB:1GHJ" FT STRAND 17..19 FT /evidence="ECO:0007829|PDB:1GHJ" FT STRAND 28..30 FT /evidence="ECO:0007829|PDB:1GHJ" FT STRAND 35..40 FT /evidence="ECO:0007829|PDB:1GHJ" FT STRAND 45..49 FT /evidence="ECO:0007829|PDB:1GHJ" FT STRAND 54..61 FT /evidence="ECO:0007829|PDB:1GHJ" FT STRAND 72..76 FT /evidence="ECO:0007829|PDB:1GHJ" SQ SEQUENCE 399 AA; 42003 MW; 3A801A1B519E73D3 CRC64; MAIDIKAPTF PESIADGTVA TWHKKPGEPV KRDELIVDIE TDKVVMEVLA EADGVIAEIV KNEGDTVLSG ELLGKLTEGG AATAAPAAAP APAAAAPAAA EAPILSPAAR KIAEENAIAA DSITGTGKGG RVTKEDAVAA AEAKKSAPAG QPAPAATAAP LFAAGDRVEK RVPMTRLRAK VAERLVEAQS SMAMLTTFNE VNMKPVMELR AKYKDLFEKT HNGVRLGFMS FFVKAAVEAL KRQPGVNASI DGNDIVYHGY QDIGVAVSSD RGLVVPVLRN AEFMSLAEIE GGINEFGKKA KAGKLTIEEM TGGTFTISNG GVFGSLLSTP IVNPPQTAIL GMHKIQERPM AVNGQVVILP MMYLALSYDH RLIDGKEAVT FLVTMKDLLE DPARLLLDV //