ID   ODO1_LEPIN              Reviewed;         920 AA.
AC   Q8F6S7;
DT   24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   04-NOV-2008, entry version 35.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component;
DE            EC=1.2.4.2;
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase;
GN   Name=sucA; Synonyms=odhA; OrderedLocusNames=LA_1224;
OS   Leptospira interrogans.
OC   Bacteria; Spirochaetes; Spirochaetales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=173;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601 / Serogroup Icterohaemorrhagiae / Serovar lai;
RX   MEDLINE=22598143; PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H.,
RA   Zhang Y.-X., Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F.,
RA   Jiang J.-X., Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F.,
RA   Zhang Y., Zhu G.-F., Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W.,
RA   Yao Z.-J., Shen Y., Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A.,
RA   Saint Girons I., Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z.,
RA   Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira
RT   interrogans revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
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: 2-oxoglutarate + [dihydrolipoyllysine-residue
CC       succinyltransferase] lipoyllysine = [dihydrolipoyllysine-residue
CC       succinyltransferase] S-succinyldihydrolipoyllysine + CO(2).
CC   -!- COFACTOR: Thiamine pyrophosphate (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase
CC       family.
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DR   EMBL; AE010300; AAN48423.1; -; Genomic_DNA.
DR   RefSeq; NP_711405.1; -.
DR   GeneID; 1150567; -.
DR   GenomeReviews; AE010300_GR; LA_1224.
DR   KEGG; lil:LA1224; -.
DR   HOGENOM; Q8F6S7; -.
DR   BioCyc; LINT189518:LA1224-MON; -.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transf...; IEA:HAMAP.
DR   GO; GO:0030976; F:thiamin pyrophosphate binding; IEA:HAMAP.
DR   GO; GO:0006096; P:glycolysis; IEA:HAMAP.
DR   GO; GO:0055114; P:oxidation reduction; IEA:UniProtKB-KW.
DR   HAMAP; MF_01169; -; 1.
DR   InterPro; IPR011603; 2oxoglutarate_DHase_E1.
DR   InterPro; IPR001017; DHase_E1.
DR   InterPro; IPR005475; Transketo_Cen_R.
DR   PANTHER; PTHR23152; 2oxoglutarate_DH_E1; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE   3: Inferred from homology;
KW   Complete proteome; Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT   CHAIN         1    920       2-oxoglutarate dehydrogenase E1
FT                                component.
FT                                /FTId=PRO_0000162174.
SQ   SEQUENCE   920 AA;  103922 MW;  8A4513F3F1B3DD0A CRC64;
     MKIEKLMALY GENGALLEEL YNQYKLNPET LDKEWKSFFQ EVDTNGLANG SGYTNGNGKS
     AVATSFTDAQ AASIREMGII NLLNAYRRQG HLAAKLDPLG IQKPNRTFID SKLHNISPAD
     IDTVVDSETL GRVKLAEIVD LYEKVYCNTI GAEHFYLVND EEREWLQKKM ESPEFLAPLP
     RGIKLRLFEK LFQADYFETF LAKKYVGKKR FSLEGGESFI PLLDTIVEEA GYHQMDGLVI
     GMAHRGRLNV LVNIIEKPAS LIFAEFEEKT DKDNLSYADV KYHLGYSNSR MTTSGKEVKL
     SLAFNPSHLE CVDPVVTGSV RARQTLIGDK DRSKYMPILI HGDAAFAGQG VVAETLNLMN
     LEGYTTGGTF HIVVNNQIGF TTLPDESRST LYATDLAKGF QIPIIHVNGD DPEAVYRVVK
     LGMEYRQKFK KDFIIDLVCY RRLGHNETDE PAFTQPKMYA IIKNHPPTVK LYEKRLVEEG
     DIPQEDIDFI KNGSMHGLED SFQRAKEQDV KIRVDTMQGV WSKFSKDSLD SEPATKLLAE
     QMHGIVQALT SVPQGFTPNS KLVKLLQSRK EMAEGKIPVD WGFAEALSFG SILESGFRIR
     LSGQDSQRGT FSHRHAVLVD TNTNEKYIPL NHISSKQAKA EIINSSLSEF SVLGFEYGYS
     LSDPNALVMW EAQFGDFANS AQVIFDQFIS SSEVKWQRLS GLIMLLPHGY EGQGPEHSSA
     RLERFLQLCA LDNMQVCNLT TAAQYFHLLR RQMLRNYRKP LVIVTPKSLL RFPASLSPVE
     DILQGAFREI LIDDSGSKPD KIEKVVFSAG KVYYDLMKYK DENKIKNVAL VRVEQIYPFP
     AKEIQSSLKT FKNAKQFVWC QEEPKNQGAW FFVRERIEEL LPGNARLVYA GRHESPSPAA
     GHMKLHLQEQ DQLVLDAFQA
//