ID   ODO2_RALEH              Reviewed;         416 AA.
AC   P52993; Q0K9A1;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 1.
DT   16-JUN-2009, entry version 71.
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=sucB; Synonyms=odhB; OrderedLocusNames=H16_A2324;
OS   Ralstonia eutropha (strain ATCC 17699 / H16 / DSM 428 / Stanier 337)
OS   (Cupriavidus necator (strain ATCC 17699 / H16 / DSM 428 / Stanier
OS   337)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=381666;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=97021018; PubMed=8867378; DOI=10.1016/0378-1097(95)00487-4;
RA   Hein S., Steinbuechel A.;
RT   "Cloning and characterization of the Alcaligenes eutrophus 2-
RT   oxoglutarate dehydrogenase complex.";
RL   FEMS Microbiol. Lett. 136:231-238(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16964242; DOI=10.1038/nbt1244;
RA   Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H.,
RA   Cramm R., Eitinger T., Ewering C., Poetter M., Schwartz E.,
RA   Strittmatter A., Voss I., Gottschalk G., Steinbuechel A.,
RA   Friedrich B., Bowien B.;
RT   "Genome sequence of the bioplastic-producing 'Knallgas' bacterium
RT   Ralstonia eutropha H16.";
RL   Nat. Biotechnol. 24:1257-1262(2006).
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).
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.
CC   -!- SIMILARITY: Belongs to the 2-oxoacid dehydrogenase family.
CC   -!- SIMILARITY: Contains 1 lipoyl-binding domain.
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DR   EMBL; X91877; CAA62981.1; -; Genomic_DNA.
DR   EMBL; AM260479; CAJ93420.1; -; Genomic_DNA.
DR   PIR; T44423; T44423.
DR   RefSeq; YP_726788.1; -.
DR   HSSP; P07016; 1C4T.
DR   GeneID; 4249724; -.
DR   GenomeReviews; AM260479_GR; H16_A2324.
DR   KEGG; reh:H16_A2324; -.
DR   HOGENOM; P52993; -.
DR   OMA; P52993; LTTYNEV.
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   Gene3D; G3DSA:4.10.320.10; E3_bd; 1.
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    416       Dihydrolipoyllysine-residue
FT                                succinyltransferase component of 2-
FT                                oxoglutarate dehydrogenase complex.
FT                                /FTId=PRO_0000162253.
FT   DOMAIN        1     77       Lipoyl-binding.
FT   ACT_SITE    387    387       By similarity.
FT   ACT_SITE    391    391       By similarity.
FT   MOD_RES      44     44       N6-lipoyllysine (Potential).
SQ   SEQUENCE   416 AA;  43250 MW;  100D839352D0A8DF CRC64;
     MAIVDVKVPQ LSESVAEATM LNWKKKPGEA VAQDEILIEI ETDKVVLEVP APSAGVLSII
     VKNDGDTVVA DEIIAKIDTE ATAGAAAPAA AAPAPAAAAP APAAAVAAPA AAGGVAMPSA
     AKLMAEAGLS AGQVAGTGKD GRITKGDALA AAAAPAAKAA PAPAAAKPAL QQVSAPVDFA
     ALGDRPEERV PMSRLRARIA ERLLQSQSTN AILTTFNEVN MKPVMDLRNK YKDRFEKEHG
     VKLGFMSFFV KAAVHALKKF PLINASIDGN DIVYHGYFDI GIAVGSPRGL VVPILRNADQ
     MSLADIEKKI AEFGVKARDG KLSLEELTGG TFSISNGGVF GSMLSTPIIN PPQSAILGVH
     ATKDRPVVED GQIVIRPMNY LAMSYDHRII DGREAVLGLV AMKDALEDPA RLLLDL
//