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ODO2_RICBR
ID   ODO2_RICBR              Reviewed;         400 AA.
AC   Q1RHI5;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 96.
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; OrderedLocusNames=RBE_1098;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
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=(R)-N(6)-dihydrolipoyl-L-lysyl-[2-oxoglutarate dehydrogenase
CC         complex component E2] + succinyl-CoA = (R)-N(6)-(S(8)-
CC         succinyldihydrolipoyl)-L-lysyl-[2-oxoglutarate dehydrogenase complex
CC         component E2] + CoA; Xref=Rhea:RHEA:15213, Rhea:RHEA-COMP:10581,
CC         Rhea:RHEA-COMP:10582, ChEBI:CHEBI:57287, ChEBI:CHEBI:57292,
CC         ChEBI:CHEBI:83100, 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; CP000087; ABE05179.1; -; Genomic_DNA.
DR   RefSeq; WP_011477757.1; NC_007940.1.
DR   AlphaFoldDB; Q1RHI5; -.
DR   SMR; Q1RHI5; -.
DR   STRING; 336407.RBE_1098; -.
DR   EnsemblBacteria; ABE05179; ABE05179; RBE_1098.
DR   KEGG; rbe:RBE_1098; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_0_0_5; -.
DR   OMA; MKVPSPG; -.
DR   OrthoDB; 1626282at2; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000001951; Chromosome.
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   Gene3D; 3.30.559.10; -; 1.
DR   Gene3D; 4.10.320.10; -; 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   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   SUPFAM; SSF47005; SSF47005; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 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..400
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex"
FT                   /id="PRO_0000288095"
FT   DOMAIN          2..77
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          85..113
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        371
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   ACT_SITE        375
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   MOD_RES         43
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ   SEQUENCE   400 AA;  43078 MW;  2C8334C1FA6F9A10 CRC64;
     MGVKIIVPSL GESVTEATIA KWYKKEGDAV KTDELLLEIE TEKVTLEVNS PCNGTIGKII
     KADGANVAVG EEIGDINEGE AVATNSNEAA KPQTASQPVP EKVPKKPAVA NNTLAPSVQK
     LVTENKLDPN NIKGTGKDGR ITKGDVLETM NAPTPAATST TSSAKASEER VERVRMSRLR
     KTIAQRLKDS QNTAAILTTF NEIDMSKVIA LRGKYKDEFE KKHGVKLGFM SFFVRATIEA
     LKLIPSVNAE IDGDDLVYKN YYDIGVAVGT EQGLVVPVVR DADKMGFADI EKTIGGLAKK
     ARDGKLSMAD LSGGTFSISN GGVYGSLLST PIINPPQSGI LGLHKTEERV VAIDGKIEIR
     PMMYIALSYD HRIIDGKEAV SFLVKIKELI ESPEKLLLNL
 
 
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