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Database: UniProt
Entry: Q2YY06
LinkDB: Q2YY06
Original site: Q2YY06 
ID   ODO2_STAAB              Reviewed;         422 AA.
AC   Q2YY06;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   13-NOV-2013, entry version 67.
DE   RecName: Full=Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex;
DE            EC=2.3.1.61;
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; OrderedLocusNames=SAB1268c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus
RT   aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI80957.1; -; Genomic_DNA.
DR   RefSeq; YP_416745.1; NC_007622.1.
DR   ProteinModelPortal; Q2YY06; -.
DR   SMR; Q2YY06; 193-419.
DR   STRING; 273036.SAB1268c; -.
DR   EnsemblBacteria; CAI80957; CAI80957; SAB1268c.
DR   GeneID; 3793632; -.
DR   KEGG; sab:SAB1268c; -.
DR   PATRIC; 19523407; VBIStaAur92441_1352.
DR   eggNOG; COG0508; -.
DR   HOGENOM; HOG000281563; -.
DR   KO; K00658; -.
DR   OMA; QEDETVE; -.
DR   OrthoDB; EOG610413; -.
DR   ProtClustDB; PRK05704; -.
DR   BioCyc; SAUR273036:GJVS-1290-MONOMER; -.
DR   UniPathway; UPA00868; UER00840.
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.
DR   InterPro; IPR004167; E3-bd.
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; SSF51230; SSF51230; 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    422       Dihydrolipoyllysine-residue
FT                                succinyltransferase component of 2-
FT                                oxoglutarate dehydrogenase complex.
FT                                /FTId=PRO_0000288098.
FT   DOMAIN        2     75       Lipoyl-binding.
FT   ACT_SITE    393    393       By similarity.
FT   ACT_SITE    397    397       By similarity.
FT   MOD_RES      42     42       N6-lipoyllysine (Potential).
SQ   SEQUENCE   422 AA;  46705 MW;  F45D1227F4EC0C95 CRC64;
     MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE EAGVLSEQLA
     SEGDTVEVGQ AIAVIGEGSG NASKENSNDN TPQQNEETNN KKEETTNKSA DNAEVNQTND
     YNQQRVNATP SARRYARENG VNLAEVSPKT NDVVRKEDID KKQQAPASTQ TTQQAPAKEE
     KKYNQYPTKP VIREKMSRRK KTAAKKLLEV SNNTAMLTTF NEVDMTNVME LRKRKKEQFM
     KDHDGTKLGF MSFFTKASVA ALKKYPEVNA EIDGDDMITK QYYDIGVAVS TDDGLLVPFV
     RDCDKKNFAE IEAEIANLAV KAREKKLGLD DMVNGSFTIT NGGIFGSMMS TPIINGNQAA
     ILGMHSIITR PIAIDQDTIE NRPMMYIALS YDHRIIDGKE AVGFLKTIKE LIENPEDLLL
     ES
//
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