ID   ODO2_BACSU              Reviewed;         417 AA.
AC   P16263;
DT   01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 2.
DT   27-MAR-2024, entry version 158.
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=odhB; Synonyms=citM; OrderedLocusNames=BSU19360;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2500417; DOI=10.1128/jb.171.7.3667-3672.1989;
RA   Carlsson P., Hederstedt L.;
RT   "Genetic characterization of Bacillus subtilis odhA and odhB, encoding 2-
RT   oxoglutarate dehydrogenase and dihydrolipoamide transsuccinylase,
RT   respectively.";
RL   J. Bacteriol. 171:3667-3672(1989).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [3]
RP   SEQUENCE REVISION TO 287 AND 328.
RX   PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA   Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G., Sekowska A.,
RA   Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT   "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT   168 reference genome a decade later.";
RL   Microbiology 155:1758-1775(2009).
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; Evidence={ECO:0000250};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000250};
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}.
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DR   EMBL; M27141; AAA22629.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB13828.2; -; Genomic_DNA.
DR   PIR; B32879; B32879.
DR   RefSeq; NP_389818.2; NC_000964.3.
DR   RefSeq; WP_004399364.1; NZ_JNCM01000036.1.
DR   AlphaFoldDB; P16263; -.
DR   SMR; P16263; -.
DR   STRING; 224308.BSU19360; -.
DR   jPOST; P16263; -.
DR   PaxDb; 224308-BSU19360; -.
DR   EnsemblBacteria; CAB13828; CAB13828; BSU_19360.
DR   GeneID; 939505; -.
DR   KEGG; bsu:BSU19360; -.
DR   PATRIC; fig|224308.179.peg.2117; -.
DR   eggNOG; COG0508; Bacteria.
DR   InParanoid; P16263; -.
DR   OrthoDB; 9805770at2; -.
DR   PhylomeDB; P16263; -.
DR   BioCyc; BSUB:BSU19360-MONOMER; -.
DR   BRENDA; 2.3.1.61; 658.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransferase activity; IBA:GO_Central.
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; IBA:GO_Central.
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; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..417
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex"
FT                   /id="PRO_0000162256"
FT   DOMAIN          1..76
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   DOMAIN          123..160
FT                   /note="Peripheral subunit-binding (PSBD)"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01170"
FT   REGION          75..191
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        91..107
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        166..187
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        388
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   ACT_SITE        392
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   MOD_RES         42
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   CONFLICT        287
FT                   /note="D -> V (in Ref. 1; AAA22629)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        328
FT                   /note="Q -> E (in Ref. 1; AAA22629)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   417 AA;  46003 MW;  E736FF4383B1A966 CRC64;
     MAEIKVPELA ESISEGTIAQ WLKQPGDYVE QGEYLLELET DKVNVELTAE ESGVLQEVLK
     DSGDTVQVGE IIGTISEGAG ESSAPAPTEK TESKESVKEE KQAEPAAQEV SEEAQSEAKS
     RTIASPSARK LAREKGIDLS QVPTGDPLGR VRKQDVEAYE KPASKPAPQQ KQQPQAQKAQ
     QSFDKPVEVQ KMSRRRQTIA KRLVEVQQTS AMLTTFNEVD MTAVMNLRKR RKDQFFEQNE
     VKLGFMSFFT KAVVAALKKY PLLNAEIQGD ELIVKKFYDI GIAVAADEGL VVPVVRDADR
     LTFAGIEKEI GELAKKARNN KLTLSELQGG SFTITNGGTF GSLMSTPILN SPQVGILGMH
     KIQLRPVAID EERFENRPMM YIALSYDHRI VDGKEAVGFL VTIKNLLEDP EQLLLEG
//