ID   A0A108U552_9GAMM        Unreviewed;       944 AA.
AC   A0A108U552;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, 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=AZ78_0289 {ECO:0000313|EMBL:KWS02743.1};
OS   Lysobacter capsici AZ78.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Lysobacter.
OX   NCBI_TaxID=1444315 {ECO:0000313|EMBL:KWS02743.1, ECO:0000313|Proteomes:UP000023435};
RN   [1] {ECO:0000313|EMBL:KWS02743.1, ECO:0000313|Proteomes:UP000023435}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AZ78 {ECO:0000313|EMBL:KWS02743.1,
RC   ECO:0000313|Proteomes:UP000023435};
RX   PubMed=24762937;
RA   Puopolo G., Sonego P., Engelen K., Pertot I.;
RT   "Draft Genome Sequence of Lysobacter capsici AZ78, a Bacterium Antagonistic
RT   to Plant-Pathogenic Oomycetes.";
RL   Genome Announc. 2:0-0(2014).
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};
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KWS02743.1}.
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DR   EMBL; JAJA02000001; KWS02743.1; -; Genomic_DNA.
DR   RefSeq; WP_036104223.1; NZ_JAJA02000001.1.
DR   AlphaFoldDB; A0A108U552; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000023435; Unassembled WGS sequence.
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:KWS02743.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          595..788
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   944 AA;  103677 MW;  065493536E84C53E CRC64;
     MDSLLKQFSQ SSQLGANAAF IEDLYEQYLV DPDSVGAKWK SYFDGFKGRE AGDVPHSAAI
     ESIAQAGKAA ARGAIASPAG GPSGSDERER AVGKVITAYR SRGHLAADID PLGLLVKPDA
     PDLALGFHRL SESDQSVEFS TGGVAGQERM KLGDLLTLLK ATYTGPIGAE FMHIADAEQR
     RWMYERLETA AGKYGRSVED KKRILERLTA ADGLERYLGT KYVGQKRFSL EGGDALIPLM
     DVTIRRAGEQ GVQDVVIGMA HRGRLNVLVN TLGKPPRKLF DEFEGKFEHD EHAHTGDVKY
     HMGFSADVAT PGGPVHLALA FNPSHLEIVN PVVAGSVRSR QTRRGDKGRA QVLPILLHGD
     AAFAGQGVGM ELFQMSQARG FAVGGTVHVV INNQVGFTTS ERQDARSTLY CTDVAKMVGA
     PILHVNSDHP EAVVFCAELA LDFRQRFGRD VVIDLVCYRR HGHNEADEPA ATQPLMYQVI
     RKHKTPRELY AEQLVGEGTL KAEDAQALVD QYRDKLDAGA VTTELVEVKP DEFTIDWSKY
     LSGKLSDPVD TTFDRAKLDA LATQINAVAD TVKLHPRVAK IYEDRRKMAA GELPGDWGFA
     ENLAYASLIS EGYKLRLVGQ DSGRGTFFHR HAIQHEQTSD EYILPLRQLV KNPSDVTIID
     SLLSEEAVMA FEYGYSTADP MTLDIWEAQF GDFANGAQVV IDQFLSSGEA KWGRLCGLVL
     LLPHGYEGQG PEHSSARLER FLQLCALENM LVCVPTTPAQ AYHMIRRQMR MSTRKPLVVM
     TPKSLLRHKL AVSSLDELAD GEFQHLIPDA AANVKKVKRV VLCSGKVYYD LYEQAQKDGL
     NDVAIVRIEQ LYPFPREALA AELKRFGAAA DVVWCQEEPQ NQGAWYQIRH HLTACLGPKQ
     ALHYAGRARS PSPAAGHLAD HIAEQTKLVA DALVNSLHGE SSAE
//