ID   ODO2_RICCN              Reviewed;         395 AA.
AC   Q92J43;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   16-JUN-2009, entry version 53.
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; OrderedLocusNames=RC0226;
OS   Rickettsia conorii.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=781;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   MEDLINE=21442074; PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M.,
RA   Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL02764.1; -; Genomic_DNA.
DR   PIR; B97728; B97728.
DR   RefSeq; NP_359863.1; -.
DR   HSSP; P07016; 1C4T.
DR   GeneID; 927964; -.
DR   GenomeReviews; AE006914_GR; RC0226.
DR   KEGG; rco:RC0226; -.
DR   NMPDR; fig|272944.1.peg.226; -.
DR   HOGENOM; Q92J43; -.
DR   OMA; Q92J43; LTTYNEV.
DR   BioCyc; RCON272944:RC0226-MON; -.
DR   BRENDA; 2.3.1.61; 267518.
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    395       Dihydrolipoyllysine-residue
FT                                succinyltransferase component of 2-
FT                                oxoglutarate dehydrogenase complex.
FT                                /FTId=PRO_0000162268.
FT   DOMAIN        1     76       Lipoyl-binding.
FT   ACT_SITE    366    366       Potential.
FT   ACT_SITE    370    370       Potential.
FT   MOD_RES      43     43       N6-lipoyllysine (Potential).
SQ   SEQUENCE   395 AA;  42798 MW;  6DAB5E9A086F5A35 CRC64;
     MRVKIIVPSL GESITEATIA KWYKKQGDSV KTDELLLEIE TEKVTLEVNA PCNGTIGKIS
     KTEGANVAVG EEIGEINEGA SANTAGTNNE SAKAQAVTQP TSEKPAVANN TLAPSVQKLV
     TENKLDPNNI KGTGRDGRIT KGDVLATINT TTTSAPAISK SNEERVQRVR MSRLRKTIAQ
     RLKDSQNTAA ILTTFNEIDM SKVIALRNQY KEEFEKKHAV KLGFMSFFVK ATIEALKLIP
     SVNAEIDGDD LVYKNYYDIG VAVGTEQGLV VPVVRDADKM GFAEVEKTIG ILAKQAREGK
     LSMADLSGGT FSISNGGVYG SLLSTPIINP PQSGILGLHK TEERAVVIDG KIEIRPMMYI
     ALSYDHRIID GKEGVSFLVK IKQLIENPEK LLLNL
//