ID ODO2_ECOLI Reviewed; 405 AA. AC P0AFG6; P07016; DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 24-JAN-2024, entry version 150. DE RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex; DE EC=2.3.1.61 {ECO:0000305|PubMed:17367808}; 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; OrderedLocusNames=b0727, JW0716; OS Escherichia coli (strain K12). OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales; OC Enterobacteriaceae; Escherichia. OX NCBI_TaxID=83333; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=K12; RX PubMed=6376124; DOI=10.1111/j.1432-1033.1984.tb08200.x; RA Spencer M.E., Darlison M.G., Stephens P.E., Duckenfield I.K., Guest J.R.; RT "Nucleotide sequence of the sucB gene encoding the dihydrolipoamide RT succinyltransferase of Escherichia coli K12 and homology with the RT corresponding acetyltransferase."; RL Eur. J. Biochem. 141:361-374(1984). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=8905232; DOI=10.1093/dnares/3.3.137; RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H., RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G., RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M., RA Horiuchi T.; RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to RT the 12.7-28.0 min region on the linkage map."; RL DNA Res. 3:137-155(1996). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / MG1655 / ATCC 47076; RX PubMed=9278503; DOI=10.1126/science.277.5331.1453; RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., RA Shao Y.; RT "The complete genome sequence of Escherichia coli K-12."; RL Science 277:1453-1462(1997). RN [4] RP PROTEIN SEQUENCE OF 4-10. RC STRAIN=K12; RX PubMed=17895580; DOI=10.1266/ggs.82.291; RA Otsuka Y., Koga M., Iwamoto A., Yonesaki T.; RT "A role of RnlA in the RNase LS activity from Escherichia coli."; RL Genes Genet. Syst. 82:291-299(2007). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911; RX PubMed=16738553; DOI=10.1038/msb4100049; RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.; RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 RT and W3110."; RL Mol. Syst. Biol. 2:E1-E5(2006). RN [6] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-12. RX PubMed=6376123; DOI=10.1111/j.1432-1033.1984.tb08199.x; RA Darlison M.G., Spencer M.E., Guest J.R.; RT "Nucleotide sequence of the sucA gene encoding the 2-oxoglutarate RT dehydrogenase of Escherichia coli K12."; RL Eur. J. Biochem. 141:351-359(1984). RN [7] RP PROTEIN SEQUENCE OF 2-13. RC STRAIN=K12 / EMG2; RX PubMed=9298646; DOI=10.1002/elps.1150180807; RA Link A.J., Robison K., Church G.M.; RT "Comparing the predicted and observed properties of proteins encoded in the RT genome of Escherichia coli K-12."; RL Electrophoresis 18:1259-1313(1997). RN [8] RP IDENTIFICATION BY 2D-GEL. RX PubMed=9298644; DOI=10.1002/elps.1150180805; RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.; RT "Escherichia coli proteome analysis using the gene-protein database."; RL Electrophoresis 18:1243-1251(1997). RN [9] RP FUNCTION, CATALYTIC ACTIVITY, AND INTERACTION WITH SUCA. RX PubMed=17367808; DOI=10.1016/j.jmb.2007.01.080; RA Frank R.A., Price A.J., Northrop F.D., Perham R.N., Luisi B.F.; RT "Crystal structure of the E1 component of the Escherichia coli 2- RT oxoglutarate dehydrogenase multienzyme complex."; RL J. Mol. Biol. 368:639-651(2007). RN [10] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-148, AND IDENTIFICATION BY MASS RP SPECTROMETRY. RC STRAIN=K12 / JW1106, and K12 / MG1655 / ATCC 47076; RX PubMed=18723842; DOI=10.1074/mcp.m800187-mcp200; RA Zhang J., Sprung R., Pei J., Tan X., Kim S., Zhu H., Liu C.F., RA Grishin N.V., Zhao Y.; RT "Lysine acetylation is a highly abundant and evolutionarily conserved RT modification in Escherichia coli."; RL Mol. Cell. Proteomics 8:215-225(2009). RN [11] RP STRUCTURE BY NMR OF 1-81, AND LIPOYLATION AT LYS-44. RX PubMed=8950276; DOI=10.1006/jmbi.1996.0632; RA Ricaud P.M., Howard M.J., Roberts E.L., Broadhurst R.W., Perham R.N.; RT "Three-dimensional structure of the lipoyl domain from the dihydrolipoyl RT succinyltransferase component of the 2-oxoglutarate dehydrogenase RT multienzyme complex of Escherichia coli."; RL J. Mol. Biol. 264:179-190(1996). RN [12] RP STRUCTURE BY NMR OF 104-153. RX PubMed=1554728; DOI=10.1021/bi00128a021; RA Robien M.A., Clore G.M., Omichinski J.G., Perham R.N., Appella E., RA Sakaguchi K., Gronenborn A.M.; RT "Three-dimensional solution structure of the E3-binding domain of the RT dihydrolipoamide succinyltransferase core from the 2-oxoglutarate RT dehydrogenase multienzyme complex of Escherichia coli."; RL Biochemistry 31:3463-3471(1992). RN [13] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 173-405, SUBUNIT, AND ACTIVE SITE. RX PubMed=9677295; DOI=10.1006/jmbi.1998.1924; RA Knapp J.E., Mitchell D.T., Yazdi M.A., Ernst S.R., Reed L.J., Hackert M.L.; RT "Crystal structure of the truncated cubic core component of the Escherichia RT coli 2-oxoglutarate dehydrogenase multienzyme complex."; RL J. Mol. Biol. 280:655-668(1998). RN [14] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 173-405, SUBUNIT, AND ACTIVE SITE. RX PubMed=10739245; DOI=10.1110/ps.9.1.37; RA Knapp J.E., Carroll D., Lawson J.E., Ernst S.R., Reed L.J., Hackert M.L.; RT "Expression, purification, and structural analysis of the trimeric form of RT the catalytic domain of the Escherichia coli dihydrolipoamide RT succinyltransferase."; RL Protein Sci. 9:37-48(2000). 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:0000305|PubMed:17367808}. 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:0000305|PubMed:17367808}; 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 (PubMed:9677295, PubMed:10739245). Part of the 2-oxoglutarate CC dehydrogenase (OGDH) complex composed of E1 (2-oxoglutarate CC dehydrogenase), E2 (dihydrolipoamide succinyltransferase) and E3 CC (dihydrolipoamide dehydrogenase); the complex contains multiple copies CC of the three enzymatic components (E1, E2 and E3) (Probable). Interacts CC with SucA (via N-terminus), the E1 component of OGDH complex CC (PubMed:17367808). {ECO:0000269|PubMed:10739245, CC ECO:0000269|PubMed:17367808, ECO:0000269|PubMed:9677295, CC ECO:0000305|PubMed:17367808}. CC -!- INTERACTION: CC P0AFG6; P0A9P0: lpdA; NbExp=3; IntAct=EBI-558621, EBI-542856; CC P0AFG6; P0AFG3: sucA; NbExp=7; IntAct=EBI-558621, EBI-543523; CC P0AFG6; P77717: ybaY; NbExp=3; IntAct=EBI-558621, EBI-558645; 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; J01619; AAA23898.1; -; Genomic_DNA. DR EMBL; X00664; CAA25284.1; -; Genomic_DNA. DR EMBL; U00096; AAC73821.1; -; Genomic_DNA. DR EMBL; AP009048; BAA35393.1; -; Genomic_DNA. DR EMBL; X00661; CAA25281.1; -; Genomic_DNA. DR PIR; F64808; XUECSD. DR RefSeq; NP_415255.1; NC_000913.3. DR RefSeq; WP_000099823.1; NZ_SSZK01000033.1. DR PDB; 1BAL; NMR; -; A=104-153. DR PDB; 1BBL; NMR; -; A=104-153. DR PDB; 1C4T; X-ray; 3.00 A; A/B/C=173-405. DR PDB; 1E2O; X-ray; 3.00 A; A=173-405. DR PDB; 1PMR; NMR; -; A=2-81. DR PDB; 1SCZ; X-ray; 2.20 A; A=173-405. DR PDB; 1W4H; NMR; -; A=109-153. DR PDB; 2BTG; NMR; -; A=109-153. DR PDB; 2BTH; NMR; -; A=109-153. DR PDB; 2WXC; NMR; -; A=109-153. DR PDB; 6PBR; X-ray; 3.00 A; A/B/C/D/E/F=173-405. DR PDBsum; 1BAL; -. DR PDBsum; 1BBL; -. DR PDBsum; 1C4T; -. DR PDBsum; 1E2O; -. DR PDBsum; 1PMR; -. DR PDBsum; 1SCZ; -. DR PDBsum; 1W4H; -. DR PDBsum; 2BTG; -. DR PDBsum; 2BTH; -. DR PDBsum; 2WXC; -. DR PDBsum; 6PBR; -. DR AlphaFoldDB; P0AFG6; -. DR BMRB; P0AFG6; -. DR SASBDB; P0AFG6; -. DR SMR; P0AFG6; -. DR BioGRID; 4259945; 23. DR BioGRID; 849684; 3. DR ComplexPortal; CPX-3921; 2-oxoglutarate dehydrogenase complex. DR DIP; DIP-35787N; -. DR IntAct; P0AFG6; 39. DR STRING; 511145.b0727; -. DR iPTMnet; P0AFG6; -. DR jPOST; P0AFG6; -. DR PaxDb; 511145-b0727; -. DR EnsemblBacteria; AAC73821; AAC73821; b0727. DR GeneID; 75205558; -. DR GeneID; 945307; -. DR KEGG; ecj:JW0716; -. DR KEGG; eco:b0727; -. DR PATRIC; fig|1411691.4.peg.1546; -. DR EchoBASE; EB0973; -. DR eggNOG; COG0508; Bacteria. DR HOGENOM; CLU_016733_0_0_6; -. DR InParanoid; P0AFG6; -. DR OMA; MKVPSPG; -. DR OrthoDB; 9805770at2; -. DR PhylomeDB; P0AFG6; -. DR BioCyc; EcoCyc:E2O-MONOMER; -. DR BioCyc; MetaCyc:E2O-MONOMER; -. DR BRENDA; 1.2.1.105; 2026. DR BRENDA; 2.3.1.61; 2026. DR SABIO-RK; P0AFG6; -. DR UniPathway; UPA00868; UER00840. DR EvolutionaryTrace; P0AFG6; -. DR PRO; PR:P0AFG6; -. DR Proteomes; UP000000318; Chromosome. DR Proteomes; UP000000625; Chromosome. DR GO; GO:0005737; C:cytoplasm; IDA:ComplexPortal. DR GO; GO:0005829; C:cytosol; IDA:EcoCyc. DR GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IDA:EcoliWiki. DR GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IDA:EcoliWiki. DR GO; GO:0031405; F:lipoic acid binding; IDA:EcoliWiki. 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; IDA:ComplexPortal. 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. DR SWISS-2DPAGE; P0AFG6; -. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Acyltransferase; Direct protein sequencing; KW Lipoyl; Reference proteome; Transferase; Tricarboxylic acid cycle. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:9298646" FT CHAIN 2..405 FT /note="Dihydrolipoyllysine-residue succinyltransferase FT component of 2-oxoglutarate dehydrogenase complex" FT /id="PRO_0000162262" FT DOMAIN 3..78 FT /note="Lipoyl-binding" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066" FT DOMAIN 113..150 FT /note="Peripheral subunit-binding (PSBD)" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01170" FT REGION 75..111 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 153..178 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 93..111 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 376 FT /evidence="ECO:0000305|PubMed:10739245, FT ECO:0000305|PubMed:9677295" FT ACT_SITE 380 FT /evidence="ECO:0000305|PubMed:10739245, FT ECO:0000305|PubMed:9677295" FT MOD_RES 44 FT /note="N6-lipoyllysine" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01066, FT ECO:0000269|PubMed:8950276" FT MOD_RES 148 FT /note="N6-acetyllysine" FT /evidence="ECO:0000269|PubMed:18723842" FT STRAND 31..34 FT /evidence="ECO:0007829|PDB:1PMR" FT STRAND 42..44 FT /evidence="ECO:0007829|PDB:1PMR" FT STRAND 70..76 FT /evidence="ECO:0007829|PDB:1PMR" FT STRAND 105..107 FT /evidence="ECO:0007829|PDB:1BAL" FT HELIX 116..118 FT /evidence="ECO:0007829|PDB:1BAL" FT HELIX 121..124 FT /evidence="ECO:0007829|PDB:1BAL" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:1BBL" FT STRAND 136..139 FT /evidence="ECO:0007829|PDB:2BTH" FT HELIX 143..146 FT /evidence="ECO:0007829|PDB:1BAL" FT TURN 147..149 FT /evidence="ECO:0007829|PDB:1BAL" FT STRAND 176..178 FT /evidence="ECO:0007829|PDB:1C4T" FT HELIX 183..196 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 201..209 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 211..228 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 235..248 FT /evidence="ECO:0007829|PDB:1SCZ" FT TURN 250..253 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 255..257 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 260..262 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 269..271 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 273..275 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 278..280 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 292..305 FT /evidence="ECO:0007829|PDB:1SCZ" FT TURN 306..309 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 313..316 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 320..325 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 326..329 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 332..334 FT /evidence="ECO:0007829|PDB:6PBR" FT STRAND 343..358 FT /evidence="ECO:0007829|PDB:1SCZ" FT STRAND 361..375 FT /evidence="ECO:0007829|PDB:1SCZ" FT TURN 376..378 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 381..396 FT /evidence="ECO:0007829|PDB:1SCZ" FT HELIX 400..403 FT /evidence="ECO:0007829|PDB:1SCZ" SQ SEQUENCE 405 AA; 44011 MW; 8439E48C6D381277 CRC64; MSSVDILVPD LPESVADATV ATWHKKPGDA VVRDEVLVEI ETDKVVLEVP ASADGILDAV LEDEGTTVTS RQILGRLREG NSAGKETSAK SEEKASTPAQ RQQASLEEQN NDALSPAIRR LLAEHNLDAS AIKGTGVGGR LTREDVEKHL AKAPAKESAP AAAAPAAQPA LAARSEKRVP MTRLRKRVAE RLLEAKNSTA MLTTFNEVNM KPIMDLRKQY GEAFEKRHGI RLGFMSFYVK AVVEALKRYP EVNASIDGDD VVYHNYFDVS MAVSTPRGLV TPVLRDVDTL GMADIEKKIK ELAVKGRDGK LTVEDLTGGN FTITNGGVFG SLMSTPIINP PQSAILGMHA IKDRPMAVNG QVEILPMMYL ALSYDHRLID GRESVGFLVT IKELLEDPTR LLLDV //