ID   ODO2_PSEPU              Reviewed;          58 AA.
AC   P31051;
DT   01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   25-MAY-2022, entry version 93.
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;
DE   Flags: Fragment;
GN   Name=sucB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=G2;
RX   PubMed=1902462; DOI=10.1128/jb.173.10.3109-3116.1991;
RA   Palmer J.A., Hatter K., Sokatch J.R.;
RT   "Cloning and sequence analysis of the LPD-glc structural gene of
RT   Pseudomonas putida.";
RL   J. Bacteriol. 173:3109-3116(1991).
RN   [2]
RP   SEQUENCE REVISION.
RA   Sokatch J.R.;
RL   Submitted (DEC-1994) to the EMBL/GenBank/DDBJ databases.
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; M80189; AAA96436.1; -; Genomic_DNA.
DR   AlphaFoldDB; P31051; -.
DR   SMR; P31051; -.
DR   STRING; 1240350.AMZE01000031_gene1966; -.
DR   eggNOG; COG0508; Bacteria.
DR   UniPathway; UPA00868; UER00840.
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   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipoyl; Transferase; Tricarboxylic acid cycle.
FT   CHAIN           <1..58
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex"
FT                   /id="PRO_0000162265"
FT   ACT_SITE        29
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   ACT_SITE        33
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   NON_TER         1
SQ   SEQUENCE   58 AA;  6691 MW;  36EC244AA98374E3 CRC64;
     MHNIIQRPMA INGQVVIRPM MYLALSYDHR LIDGKEAVTF LVTIKNLLED PSRLLLDI