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 28-MAR-2018, entry version 91.
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; Staphylococcaceae;
OC 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). {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY: Succinyl-CoA + enzyme N(6)-
CC (dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-
CC succinyldihydrolipoyl)lysine.
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
CC saccharopine pathway; glutaryl-CoA from L-lysine: step 6/6.
CC -!- SUBUNIT: Forms a 24-polypeptide structural core with octahedral
CC symmetry. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC {ECO:0000305}.
DR EMBL; AJ938182; CAI80957.1; -; Genomic_DNA.
DR RefSeq; WP_001115457.1; NC_007622.1.
DR ProteinModelPortal; Q2YY06; -.
DR SMR; Q2YY06; -.
DR EnsemblBacteria; CAI80957; CAI80957; SAB1268c.
DR KEGG; sab:SAB1268c; -.
DR HOGENOM; HOG000281563; -.
DR KO; K00658; -.
DR OMA; MKVPSPG; -.
DR BioCyc; SAUR273036:G1G1D-1411-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_sf.
DR InterPro; IPR036625; E3-bd_dom_sf.
DR InterPro; IPR004167; PSBD.
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.
DR PROSITE; PS51826; PSBD; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Lipoyl; Transferase; Tricarboxylic acid cycle.
FT CHAIN 1 422 Dihydrolipoyllysine-residue
FT succinyltransferase component of 2-
FT oxoglutarate dehydrogenase complex.
FT /FTId=PRO_0000288098.
FT DOMAIN 1 76 Lipoyl-binding. {ECO:0000255|PROSITE-
FT ProRule:PRU01066}.
FT DOMAIN 127 163 Peripheral subunit-binding (PSBD).
FT {ECO:0000255|PROSITE-ProRule:PRU01170}.
FT ACT_SITE 393 393 {ECO:0000250}.
FT ACT_SITE 397 397 {ECO:0000250}.
FT MOD_RES 42 42 N6-lipoyllysine. {ECO:0000255|PROSITE-
FT ProRule:PRU01066}.
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
//
