ID   M1LUK0_9PROT            Unreviewed;       957 AA.
AC   M1LUK0;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=CDSE_0714 {ECO:0000313|EMBL:AGF46989.1};
OS   Candidatus Kinetoplastibacterium desouzaii TCC079E.
OC   Bacteria; Pseudomonadota; Betaproteobacteria;
OC   Candidatus Kinetoplastibacterium.
OX   NCBI_TaxID=1208919 {ECO:0000313|EMBL:AGF46989.1, ECO:0000313|Proteomes:UP000011547};
RN   [1] {ECO:0000313|EMBL:AGF46989.1, ECO:0000313|Proteomes:UP000011547}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TCC079E {ECO:0000313|EMBL:AGF46989.1,
RC   ECO:0000313|Proteomes:UP000011547};
RX   PubMed=23345457;
RA   Alves J.M., Serrano M.G., Maia da Silva F., Voegtly L.J., Matveyev A.V.,
RA   Teixeira M.M., Camargo E.P., Buck G.A.;
RT   "Genome evolution and phylogenomic analysis of candidatus
RT   kinetoplastibacterium, the betaproteobacterial endosymbionts of strigomonas
RT   and angomonas.";
RL   Genome Biol. Evol. 5:338-350(2013).
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:0000256|ARBA:ARBA00003906}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP003803; AGF46989.1; -; Genomic_DNA.
DR   RefSeq; WP_015396400.1; NC_020294.1.
DR   AlphaFoldDB; M1LUK0; -.
DR   STRING; 1208919.CDSE_0714; -.
DR   KEGG; kde:CDSE_0714; -.
DR   PATRIC; fig|1208919.3.peg.428; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000011547; Chromosome.
DR   GO; GO:0004591; F:oxoglutarate dehydrogenase (succinyl-transferring) activity; IEA:UniProtKB-EC.
DR   GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro.
DR   GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro.
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   InterPro; IPR032106; 2-oxogl_dehyd_N.
DR   InterPro; IPR011603; 2oxoglutarate_DH_E1.
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   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          603..800
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   957 AA;  107784 MW;  0FEC8A686C61629D CRC64;
     MSSNKESLST SYLFGGNAPY VEELYEIYLD NPGAVAEHWR QYFDNLQNSP ATDGSEATRD
     QIHSPIVESF AQRAKSNSFV SKSSTNQDLS VASKQVFVQS LIAAYRSLGI HWADLDPLKR
     KERVEIKELE PSFYGFTEAD LDQVYSCSNT YFTKSSTMTL RDILKALRDT YCRSIGVEFM
     HVSDPSIKRW IQERMESTHG VDININSDSK RHILQQLTEA EGLERFLHTK YVGQKRFSLE
     GGESFIASMD EVVNHSADLG VQEIIVGMAH RGRLNMLVNI MGKMPGDLFA EFEGKHSQSL
     ADGDVKYHNG FSSDLATRSG PVHLSLSFNP SHLEIVNPVV EGSARARQER RADYKGKQVL
     PVLVHGDSAF SGQGVVMETL NLAQTRGYGT GGTIHLVINN QIGFTTSDPR DSRSTIYCTD
     VVKMIEAPVF HVNGDDPEAV VFATRLAVDY RMQFGRDVVV DIVCFRKLGH NEQDTPALTQ
     PLMYKRIVKH PGTRKLYADK LIAQQVITTE EADSLVKDYR QVMEDGHRTI EPILTDYKSK
     YAIDWVPFLN SKWTDHADTA LPISELKRIG ELITKVPDGF NTHSLVAKLL NDRRKMSQGE
     INLDYGMGEH LAFASLLLSG YGVRITGQDS GRGTFTHRHA VLHDQNRERW DDGTYIPLQN
     LSDTQAPFVV IDSVLSEEAV LGFEYGYACS EPNTLTIWEA QFGDFVNGAQ VVIDQFISSG
     ESKWGRQSGL TMMLPHGYEG QGPEHSSARI ERFLQLCADN NMQVVQPTDA SQIFHVLRRQ
     MIRPFRKPLV LFTPKSLLRN KDASSPLSDI SEGSFKTIIP EVDKNINQKS VKRLLVCSGK
     VYYDLANARR DRSIDNVAII RVEQLYPFAH KAFEFELSKY PNLTEIIWVQ DEPQNQGPWY
     YIQHHLYENM IDGQKLGYAG RNASASPAVG YLAKHQEQQK ALVDQAFAQK FKVILAK
//