ID   ODO2_STAES              Reviewed;         420 AA.
AC   Q8CSL9;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   16-JUN-2009, entry version 44.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE            Short=E2;
DE            EC=2.3.1.61;
DE   AltName: Full=Dihydrolipoamide succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
GN   Name=odhB; Synonyms=sucB; OrderedLocusNames=SE_1096;
OS   Staphylococcus epidermidis (strain ATCC 12228).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   MEDLINE=22832016; PubMed=12950922;
RX   DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J.,
RA   Qin Z.-Q., Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z.,
RA   Yuan Z.-H., Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: The 2-oxoglutarate dehydrogenase complex catalyzes the
CC       overall conversion of 2-oxoglutarate to succinyl-CoA and CO(2). It
CC       contains multiple copies of three enzymatic components: 2-
CC       oxoglutarate dehydrogenase (E1), dihydrolipoamide
CC       succinyltransferase (E2) and lipoamide dehydrogenase (E3) (By
CC       similarity).
CC   -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
CC       (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
CC       succinyldihydrolipoyl)lysine.
CC   -!- COFACTOR: Binds 1 lipoyl cofactor covalently (By similarity).
CC   -!- PATHWAY: Amino-acid degradation; L-lysine degradation via
CC       saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC   -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC       symmetry (By similarity).
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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DR   EMBL; AE015929; AAO04693.1; -; Genomic_DNA.
DR   RefSeq; NP_764651.1; -.
DR   HSSP; P07016; 1C4T.
DR   GeneID; 1057477; -.
DR   GenomeReviews; AE015929_GR; SE_1096.
DR   KEGG; sep:SE1096; -.
DR   HOGENOM; Q8CSL9; -.
DR   OMA; Q8CSL9; LTTYNEV.
DR   BioCyc; SEPI176280:SE_1096-MON; -.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IEA:InterPro.
DR   GO; GO:0004149; F:dihydrolipoyllysine-residue succinyltransfe...; IEA:EC.
DR   GO; GO:0031405; F:lipoic acid binding; IEA:UniProtKB-KW.
DR   GO; GO:0005515; F:protein binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW.
DR   InterPro; IPR003016; 2-oxoA_DH_lipoyl-BS.
DR   InterPro; IPR001078; 2-oxoacid_DH_actylTfrase.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR004167; E3_bd.
DR   InterPro; IPR006255; SucB.
DR   Pfam; PF00198; 2-oxoacid_dh; 1.
DR   Pfam; PF00364; Biotin_lipoyl; 1.
DR   Pfam; PF02817; E3_binding; 1.
DR   ProDom; PD001115; 2Oxoacid_dh; 1.
DR   TIGRFAMs; TIGR01347; sucB; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00189; LIPOYL; 1.
PE   3: Inferred from homology;
KW   Acyltransferase; Complete proteome; Lipoyl; Transferase;
KW   Tricarboxylic acid cycle.
FT   CHAIN         1    420       Dihydrolipoyllysine-residue
FT                                succinyltransferase component of 2-
FT                                oxoglutarate dehydrogenase complex.
FT                                /FTId=PRO_0000288107.
FT   DOMAIN        2     75       Lipoyl-binding.
FT   ACT_SITE    391    391       By similarity.
FT   ACT_SITE    395    395       By similarity.
FT   MOD_RES      42     42       N6-lipoyllysine (Potential).
SQ   SEQUENCE   420 AA;  46066 MW;  6F1F51E5923A2F64 CRC64;
     MAEVKVPELA ESITEGTIAE WLKNVGDNVD KGEAILELET DKVNVEVVSE EAGVLSEQLA
     EEGDTVEVGQ AVAVVGEGQV NTSNDSSNES SQKDEAKEKE TPKQSNPNSS ESENTQDNSQ
     QRINATPSAR RHARKNGVDL SEVSGKGNDV LRKDDVENSQ KSSSQTAKSE SKSQNSGSKQ
     SNNNPSKPVI REKMSRRKKT AAKKLLEVSN QTAMLTTFNE VDMTNVMDLR KRKKEQFIKD
     HDGTKLGFMS FFTKAAVAAL KKYPEVNAEI DGDDMITKQF YDIGIAVSTD DGLLVPFVRD
     CDKKNFAEIE QEIANLAVKA RDKKLGLDDM VNGSFTITNG GIFGSMMSTP IINGNQAAIL
     GMHSIITRPI AVDKDTIENR PMMYIALSYD HRIIDGKEAV GFLKTIKELI ENPEDLLLES
//