ID   A0A068QQW5_9GAMM        Unreviewed;       935 AA.
AC   A0A068QQW5;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:CDG17041.1};
GN   ORFNames=XDD1_1342 {ECO:0000313|EMBL:CDG17041.1};
OS   Xenorhabdus doucetiae.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Morganellaceae; Xenorhabdus.
OX   NCBI_TaxID=351671 {ECO:0000313|EMBL:CDG17041.1, ECO:0000313|Proteomes:UP000032721};
RN   [1] {ECO:0000313|EMBL:CDG17041.1, ECO:0000313|Proteomes:UP000032721}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FRM16 / DSM 17909 {ECO:0000313|Proteomes:UP000032721};
RA   Genoscope - CEA;
RL   Submitted (JUL-2013) 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; FO704550; CDG17041.1; -; Genomic_DNA.
DR   RefSeq; WP_045969647.1; NZ_VNHN01000008.1.
DR   AlphaFoldDB; A0A068QQW5; -.
DR   STRING; 351671.XDD1_1342; -.
DR   KEGG; xdo:XDD1_1342; -.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000032721; 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:CDG17041.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          593..786
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   935 AA;  105209 MW;  FAC2CD289C15B0E6 CRC64;
     MQNGAMKDWL DSSFLAGANQ SYIEQIYEDY ITDPNSVDAS WREIFQQLPD AGFGGEQLHS
     QTRDYFRRLA KDATRYHTSV SDPAMDAKQV KVLQLINAFR FRGHQHANLD PLGLWKQEPV
     SDLDPAFHNL TKADFEETFN VGSFAIGKET MKLADLYDAL RRIYCGSIGA EYMHITNTEE
     KRWIQQRLES VTVSSQFNAE EKRRFLKELT AAEGLERYLG AKFPGAKRFS LEGGDALIPM
     LKELIRHAGK QDTREVVLGM AHRGRLNVLV NLLGKKPGDL FDEFAGKHKE HLGTGDVKYH
     QGFSSDFETE GGLVHLALAF NPSHLEIVSP VVIGSVRARR DRLDEGRSNM VLPVTIHGDA
     AVTGQGIVQE TLNMSQARGY EVGGTVRIVV NNQIGFTTSN PKDARSTQYC TDVVKMVQAP
     IFHVNADDPE AVAFVTRLAL DFRNTFKRDV MIDLVCYRRH GHNEADEPSA TQPLMYQKIK
     KLPTARKIYA DKLVAEGLLG ANDVTEMVNL YRDALDHGEC VVDEWRPMGL HSFTWEPYLN
     HEWDEEYPHK VDMKRLQDLG KSISTVPAEI EMHSRVAKIY GDRAEMANGN KLFDWGGAET
     LAYATLVDEG IPVRLSGEDA GRGTFFHRHA VVHNQNNASV YVPLANIHNG QGVFNVWDSV
     LSEEAVLAFE YGYATTEPRA LTIWEAQFGD FANVAQVVID QFISSGEQKW GRMCGLVMLL
     PHGYEGQGPE HSSARLERYL QLCAEQNMQV CVPSTPAQVY HMLRRQALRG MRRPLIVMSP
     KSLLRHPLAV SSLDELANGK FEPVIGEVDA LAPKGVKRVV LCSGKVYYDL LEQRRKNEQT
     DVAIVRIEQL YPFPRQHLQA QLEQYAHVHD FVWCQEEPLN QGAWYCSQHN FREAIPFGAS
     LRYAGRPASA SPAVGYPSVH QQQQQALVND ALNVE
//