ODO1_LEPIC
ID ODO1_LEPIC Reviewed; 920 AA.
AC Q72PJ7;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 25-MAY-2022, entry version 98.
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=LIC_12474;
OS Leptospira interrogans serogroup Icterohaemorrhagiae serovar copenhageni
OS (strain Fiocruz L1-130).
OC Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX NCBI_TaxID=267671;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fiocruz L1-130;
RX PubMed=15028702; DOI=10.1128/jb.186.7.2164-2172.2004;
RA Nascimento A.L.T.O., Ko A.I., Martins E.A.L., Monteiro-Vitorello C.B.,
RA Ho P.L., Haake D.A., Verjovski-Almeida S., Hartskeerl R.A., Marques M.V.,
RA Oliveira M.C., Menck C.F.M., Leite L.C.C., Carrer H., Coutinho L.L.,
RA Degrave W.M., Dellagostin O.A., El-Dorry H., Ferro E.S., Ferro M.I.T.,
RA Furlan L.R., Gamberini M., Giglioti E.A., Goes-Neto A., Goldman G.H.,
RA Goldman M.H.S., Harakava R., Jeronimo S.M.B., Junqueira-de-Azevedo I.L.M.,
RA Kimura E.T., Kuramae E.E., Lemos E.G.M., Lemos M.V.F., Marino C.L.,
RA Nunes L.R., de Oliveira R.C., Pereira G.G., Reis M.S., Schriefer A.,
RA Siqueira W.J., Sommer P., Tsai S.M., Simpson A.J.G., Ferro J.A.,
RA Camargo L.E.A., Kitajima J.P., Setubal J.C., Van Sluys M.A.;
RT "Comparative genomics of two Leptospira interrogans serovars reveals novel
RT insights into physiology and pathogenesis.";
RL J. Bacteriol. 186:2164-2172(2004).
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=(R)-N(6)-lipoyl-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + 2-oxoglutarate + H(+) = (R)-N(6)-(S(8)-
CC succinyldihydrolipoyl)-L-lysyl-[dihydrolipoyllysine-residue
CC succinyltransferase] + CO2; Xref=Rhea:RHEA:12188, Rhea:RHEA-
CC COMP:10483, Rhea:RHEA-COMP:10484, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:16526, ChEBI:CHEBI:16810, ChEBI:CHEBI:83099,
CC ChEBI:CHEBI:83120; EC=1.2.4.2; Evidence={ECO:0000255|HAMAP-
CC 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; AE016823; AAS71039.1; -; Genomic_DNA.
DR RefSeq; WP_000687652.1; NC_005823.1.
DR AlphaFoldDB; Q72PJ7; -.
DR SMR; Q72PJ7; -.
DR PaxDb; Q72PJ7; -.
DR EnsemblBacteria; AAS71039; AAS71039; LIC_12474.
DR GeneID; 61142351; -.
DR KEGG; lic:LIC_12474; -.
DR HOGENOM; CLU_004709_1_0_12; -.
DR OMA; RDSYCRT; -.
DR Proteomes; UP000007037; Chromosome I.
DR GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-UniRule.
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; IEA:InterPro.
DR Gene3D; 3.40.50.11610; -; 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 PANTHER; PTHR23152; PTHR23152; 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; SSF52518; 2.
DR TIGRFAMs; TIGR00239; 2oxo_dh_E1; 1.
PE 3: Inferred from homology;
KW Glycolysis; Oxidoreductase; Thiamine pyrophosphate.
FT CHAIN 1..920
FT /note="2-oxoglutarate dehydrogenase E1 component"
FT /id="PRO_0000162173"
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
