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   27-MAR-2024, entry version 111.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000255|HAMAP-Rule:MF_01169};
DE            EC=1.2.4.2 {ECO:0000255|HAMAP-Rule:MF_01169};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Name=sucA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   Synonyms=odhA {ECO:0000255|HAMAP-Rule:MF_01169};
GN   OrderedLocusNames=LA_1224;
OS   Leptospira interrogans serogroup Icterohaemorrhagiae serovar Lai (strain
OS   56601).
OC   Bacteria; Spirochaetota; Spirochaetia; Leptospirales; Leptospiraceae;
OC   Leptospira.
OX   NCBI_TaxID=189518;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=56601;
RX   PubMed=12712204; DOI=10.1038/nature01597;
RA   Ren S.-X., Fu G., Jiang X.-G., Zeng R., Miao Y.-G., Xu H., Zhang Y.-X.,
RA   Xiong H., Lu G., Lu L.-F., Jiang H.-Q., Jia J., Tu Y.-F., Jiang J.-X.,
RA   Gu W.-Y., Zhang Y.-Q., Cai Z., Sheng H.-H., Yin H.-F., Zhang Y., Zhu G.-F.,
RA   Wan M., Huang H.-L., Qian Z., Wang S.-Y., Ma W., Yao Z.-J., Shen Y.,
RA   Qiang B.-Q., Xia Q.-C., Guo X.-K., Danchin A., Saint Girons I.,
RA   Somerville R.L., Wen Y.-M., Shi M.-H., Chen Z., Xu J.-G., Zhao G.-P.;
RT   "Unique physiological and pathogenic features of Leptospira interrogans
RT   revealed by whole-genome sequencing.";
RL   Nature 422:888-893(2003).
CC   -!- FUNCTION: E1 component of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex which catalyzes the decarboxylation of 2-oxoglutarate, the
CC       first step in the conversion of 2-oxoglutarate to succinyl-CoA and
CC       CO(2). {ECO:0000255|HAMAP-Rule:MF_01169}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2-oxoglutarate + H(+) + N(6)-[(R)-lipoyl]-L-lysyl-
CC         [dihydrolipoyllysine-residue succinyltransferase] = CO2 + N(6)-[(R)-
CC         S(8)-succinyldihydrolipoyl]-L-lysyl-[dihydrolipoyllysine-residue
CC         succinyltransferase]; Xref=Rhea:RHEA:12188, Rhea:RHEA-COMP:10483,
CC         Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:16810, ChEBI:CHEBI:83099, ChEBI:CHEBI:83120; EC=1.2.4.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01169};
CC   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000255|HAMAP-
CC       Rule:MF_01169}.
CC   -!- SIMILARITY: Belongs to the alpha-ketoglutarate dehydrogenase family.
CC       {ECO:0000255|HAMAP-Rule:MF_01169}.
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DR   EMBL; AE010300; AAN48423.1; -; Genomic_DNA.
DR   RefSeq; NP_711405.1; NC_004342.2.
DR   RefSeq; WP_000687652.1; NC_004342.2.
DR   AlphaFoldDB; Q8F6S7; -.
DR   SMR; Q8F6S7; -.
DR   STRING; 189518.LA_1224; -.
DR   PaxDb; 189518-LA_1224; -.
DR   EnsemblBacteria; AAN48423; AAN48423; LA_1224.
DR   GeneID; 61142351; -.
DR   KEGG; lil:LA_1224; -.
DR   PATRIC; fig|189518.3.peg.1221; -.
DR   HOGENOM; CLU_004709_1_0_12; -.
DR   InParanoid; Q8F6S7; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000001408; Chromosome I.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0045252; C:oxoglutarate dehydrogenase complex; IBA:GO_Central.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IBA:GO_Central.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central.
DR   CDD; cd02016; TPP_E1_OGDC_like; 1.
DR   Gene3D; 3.40.50.12470; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
DR   Gene3D; 3.40.50.11610; Multifunctional 2-oxoglutarate metabolism enzyme, C-terminal domain; 1.
DR   Gene3D; 1.10.287.1150; TPP helical domain; 1.
DR   HAMAP; MF_01169; SucA_OdhA; 1.
DR   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
DR   InterPro; IPR023784; 2oxoglutarate_DH_E1_bac.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR031717; KGD_C.
DR   InterPro; IPR042179; KGD_C_sf.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   NCBIfam; TIGR00239; 2oxo_dh_E1; 1.
DR   PANTHER; PTHR23152:SF4; 2-OXOADIPATE DEHYDROGENASE COMPLEX COMPONENT E1; 1.
DR   PANTHER; PTHR23152; 2-OXOGLUTARATE DEHYDROGENASE; 1.
DR   Pfam; PF16078; 2-oxogl_dehyd_N; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF16870; OxoGdeHyase_C; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   PIRSF; PIRSF000157; Oxoglu_dh_E1; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   3: Inferred from homology;
KW   Glycolysis; Oxidoreductase; Reference proteome; Thiamine pyrophosphate.
FT   CHAIN           1..920
FT                   /note="2-oxoglutarate dehydrogenase E1 component"
FT                   /id="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
//