ID   ODO2_BUCAI              Reviewed;         420 AA.
AC   P57389;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2000, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=BU303;
OS   Buchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon
OS   pisum symbiotic bacterium).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=107806;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=APS;
RX   PubMed=10993077; DOI=10.1038/35024074;
RA   Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.;
RT   "Genome sequence of the endocellular bacterial symbiont of aphids Buchnera
RT   sp. APS.";
RL   Nature 407:81-86(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: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; BA000003; BAB13012.1; -; Genomic_DNA.
DR   RefSeq; NP_240126.1; NC_002528.1.
DR   RefSeq; WP_010896058.1; NC_002528.1.
DR   AlphaFoldDB; P57389; -.
DR   SMR; P57389; -.
DR   STRING; 107806.10038977; -.
DR   PRIDE; P57389; -.
DR   EnsemblBacteria; BAB13012; BAB13012; BAB13012.
DR   KEGG; buc:BU303; -.
DR   PATRIC; fig|107806.10.peg.314; -.
DR   eggNOG; COG0508; Bacteria.
DR   HOGENOM; CLU_016733_0_0_6; -.
DR   OMA; MKVPSPG; -.
DR   UniPathway; UPA00868; UER00840.
DR   Proteomes; UP000001806; 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   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR023213; CAT-like_dom_sf.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   InterPro; IPR006255; SucB.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   SUPFAM; SSF51230; SSF51230; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Lipoyl; Reference proteome; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN           1..420
FT                   /note="Dihydrolipoyllysine-residue succinyltransferase
FT                   component of 2-oxoglutarate dehydrogenase complex"
FT                   /id="PRO_0000162259"
FT   DOMAIN          3..78
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   ACT_SITE        391
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   ACT_SITE        395
FT                   /evidence="ECO:0000250|UniProtKB:P0AFG6"
FT   MOD_RES         44
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
SQ   SEQUENCE   420 AA;  48092 MW;  E0028D647A5CE34C CRC64;
     MKKINILVPD LPESISDATV VKWHKKIGDT VHCDDNIVDI ETDKVMLEVS SPCDGILQSI
     LEKEGKVVIS QQTLGEINKS TVVDNHLSNN HIIEKEDNLL KKEEKYITTE EKKEIEYLLK
     DNHKHLTPSM RRSVKIHNIN NGFLNQVIET SKKTNFENII KEEKKESNQI LFNHNIFNAN
     ENNKNNNNKV TNRVKMTRLR QRIAERLLDS KNNTAMLTTF HEVNMKPIIL LRKKYGEDFE
     KKHNVRIGFM SFFVKAVIQA LKNFPEINAY IDQTDIVFYK NFDISIAIST PRGLITPVIR
     NADTMTMAEI EKKIKDFSIK GLQNKINIKE LMGGNFTITN GGVFGSLMST PIINPPQTAI
     LGMHVIQERP VVVNGQIKIL PMMYLALSYD HRLIDGKESV GFLINIKNIL EDFNRIAIDV