ID   A0A345ZJF4_9GAMM        Unreviewed;       942 AA.
AC   A0A345ZJF4;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=DWG18_05980 {ECO:0000313|EMBL:AXK71879.1};
OS   Lysobacter sp. TY2-98.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=2290922 {ECO:0000313|EMBL:AXK71879.1, ECO:0000313|Proteomes:UP000254438};
RN   [1] {ECO:0000313|EMBL:AXK71879.1, ECO:0000313|Proteomes:UP000254438}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TY2-98 {ECO:0000313|EMBL:AXK71879.1,
RC   ECO:0000313|Proteomes:UP000254438};
RA   Kim S.-G., Park A.-Y., Lee Y.-J.;
RT   "Lysobacter sp. nov. isolated from a farm soil.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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; CP031413; AXK71879.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A345ZJF4; -.
DR   KEGG; lyt:DWG18_05980; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000254438; 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   ECO:0000313|EMBL:AXK71879.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000254438};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          594..787
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   942 AA;  104424 MW;  4F886CDC07F59FCE CRC64;
     MDSLLKQFAQ TSQLGANAAY VEDLYEQYLV APDSVDPKWK AYFDGVKSGS TTEVPHSAVL
     ESIAEAGRQA ARGALASCGS AADERQYAVG KLIVAYRSRG HLAANLDPLG LEKMPPAPDL
     ELAFHGLSEK DLSAEFSTGG VGGKDRMKLA DLVDLLKRTY TGTVGAEFMH IAESDQRRWI
     YERMEKAGGR YARSADERKR VLERLTAADG LERYLGTKYV GQKRFSLEGG DSLIPLLDDM
     VRRAGTQDAK EIVMGMAHRG RLNVLVNTLG KPPRDLFNEF EGKFEHVHSD LAHQGDVKYH
     MGFSADVATP GGPVHLALAF NPSHLEIVDP VVAGSVRSRQ TRRGDESRKQ ILPVLMHGDA
     AFAGQGVVME LFQMSQARGF AVGGTVHIVI NNQVGFTTSE RQDARSTLYC TDVSKMVGAP
     VLHVNGDDPD AVLFCGELAL DFRNTFGKDV VIDLVCYRRH GHNEADEPAA TQPLMYQVIR
     KHPTPRELYA KRLIAENVIT EADAQAMVDA YRAKMDAGEV TAEVVDVKPD EFTPDWSSFL
     TGKLSDPVDT RFDRTKLVEL ATAINTVPDR ITLHPRVAKI YDDRRKMTAG EQPGDWGFAE
     NLAYATLLKE GYKLRLVGQD CGRGTFFHRH AILHDQKTDE YYLPLRELVG NPADVAVIDS
     LLSEEAVMAF EYGYSTADPM TLDIWEAQFG DFANGAQVVI DQFLSSGEAK WGRLCGLALY
     LPHGYEGQGP EHSSARLERY LQLCALDNMI VCTPTTPAQD FHMIRRQMRM TTRKPLVVMT
     PKSLLRHKLA VSTLDELANG EFQKLIPDSV TTPKKAKRVV ICGGKVYYDL LEDMQKRGAD
     DVALIRIEQL YPFPRNELKA ELAKYSTKDV VWCQEEPMNQ GAWYQIRHHL VACLGAKQSI
     HYAGRSRSPS PAAGHFADHV REQQQLIADA LVNPLNGEVS EE
//