ID   ODO2_STAAR              Reviewed;         423 AA.
AC   Q6GGZ6;
DT   29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   16-JUN-2009, entry version 37.
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=SAR1424;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacillales; Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T.,
RA   Churcher C., Clark L., Corton C., Cronin A., Doggett J., Dowd L.,
RA   Feltwell T., Hance Z., Harris B., Hauser H., Holroyd S., Jagels K.,
RA   James K.D., Lennard N., Line A., Mayes R., Moule S., Mungall K.,
RA   Ormond D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Sanders M.,
RA   Sharp S., Simmonds M., Stevens K., Whitehead S., Barrell B.G.,
RA   Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains:
RT   evidence for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571856; CAG40421.1; -; Genomic_DNA.
DR   RefSeq; YP_040826.1; -.
DR   GeneID; 2859175; -.
DR   GenomeReviews; BX571856_GR; SAR1424.
DR   KEGG; sar:SAR1424; -.
DR   HOGENOM; Q6GGZ6; -.
DR   OMA; Q6GGZ6; LTTYNEV.
DR   BioCyc; SAUR282458:SAR1424-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    423       Dihydrolipoyllysine-residue
FT                                succinyltransferase component of 2-
FT                                oxoglutarate dehydrogenase complex.
FT                                /FTId=PRO_0000288100.
FT   DOMAIN        2     75       Lipoyl-binding.
FT   ACT_SITE    394    394       By similarity.
FT   ACT_SITE    398    398       By similarity.
FT   MOD_RES      42     42       N6-lipoyllysine (Potential).
SQ   SEQUENCE   423 AA;  46773 MW;  50F814EE00B66830 CRC64;
     MPEVKVPELA ESITEGTIAE WLKNLGDSVE KGEAILELET DKVNVEVVSE EAGVLSEQLA
     SEGDTVEVGQ AIAVIGEGSG NASKENSNDN TPQQNDETTN NKKEETTNKS ADKAEVNQTN
     DDNQQRVNAT PSARRYAREN GVNLAEVSPK TNDVVRKEDI DKKQQAPAST QTTQQAPAKE
     EKKYNQYPTK PVIREKMSRR KKTAAKKLLE VSNNTAMLTT FNEVDMTNVM ELRKRKKEQF
     MKDHDGTKLG FMSFFTKASV AALKKYPEVN AEIDGDDMIT KQYYDIGVAV STDDGLLVPF
     VRDCDKKNFA EIEAEIANLA VKAREKKLGL DDMVNGSFTI TNGGIFGSMM STPIINGNQA
     AILGMHSIIT RPIAIDQDTI ENRPMMYIAL SYDHRIIDGK EAVGFLKTIK ELIENPEDLL
     LES
//