ID ODO2_STAHJ Reviewed; 423 AA.
AC Q4L6C3;
DT 29-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 29-MAY-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; Synonyms=sucB; OrderedLocusNames=SH1493;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/JB.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S.,
RA Lee J.C., Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04802.1; -; Genomic_DNA.
DR RefSeq; YP_253408.1; NC_007168.1.
DR ProteinModelPortal; Q4L6C3; -.
DR SMR; Q4L6C3; 194-420.
DR STRING; 279808.SH1493; -.
DR EnsemblBacteria; BAE04802; BAE04802; SH1493.
DR GeneID; 3481999; -.
DR KEGG; sha:SH1493; -.
DR PATRIC; 19619097; VBIStaHae67511_1472.
DR eggNOG; COG0508; -.
DR HOGENOM; HOG000281563; -.
DR KO; K00658; -.
DR OMA; AAMLTTY; -.
DR ProtClustDB; PRK05704; -.
DR BioCyc; SHAE279808:GJX7-1547-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: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; SSF47005; E3_bd; 1.
DR SUPFAM; SSF51230; Hybrid_motif; 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_0000288109.
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; 46249 MW; C1FD7CF93C4E1D88 CRC64;
MPEVKVPELA ESITEGTIAE WLKNVGDSVE KGEAILELET DKVNVEVVSE EEGVLQEQLA
SEGDTVEVGQ VIATVGEGSG NASSSKEESS DQSQSANNDE ATKELAQPTE SQSNNEETQS
NPNNQRVNAT PSARRHAREN GVDLSTVSGK GNDVVRKDDV ENSQKAAQSQ SSQETSKKEE
PKKSSGAPNK PVIREKMSRR KKTAAKKLLE VSNNTAMLTT FNEVDMTNVM ELRKRKKEQF
IKDHDGTKLG FMSFFTKAAV AALKKYPEVN AEIDGDDMIT KQYYDIGVAV STDDGLLVPF
VRDCDKKNFA ELERAIADLA VKARDKKLGL DDMVNGSFTI TNGGVFGSMM STPIINGNQA
AILGMHSIIT RPIAIDKDTI ENRPMMYIAL SYDHRIIDGK EAVGFLKTIK ELIESPEDLL
LES
//
