ID   D0JBQ9_BLASB            Unreviewed;       921 AA.
AC   D0JBQ9;
DT   15-DEC-2009, integrated into UniProtKB/TrEMBL.
DT   15-DEC-2009, sequence version 1.
DT   27-MAR-2024, entry version 60.
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:ACY40597.1};
GN   OrderedLocusNames=BLBBGE_597 {ECO:0000313|EMBL:ACY40597.1};
OS   Blattabacterium sp. subsp. Blattella germanica (strain Bge) (Blattella
OS   germanica symbiotic bacterium).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Blattabacteriaceae; Blattabacterium.
OX   NCBI_TaxID=331104 {ECO:0000313|EMBL:ACY40597.1, ECO:0000313|Proteomes:UP000002625};
RN   [1] {ECO:0000313|EMBL:ACY40597.1, ECO:0000313|Proteomes:UP000002625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bge {ECO:0000313|Proteomes:UP000002625};
RX   PubMed=19911043; DOI=10.1371/journal.pgen.1000721;
RA   Lopez-Sanchez M.J., Neef A., Pereto J., Patino-Navarrete R., Pignatelli M.,
RA   Latorre A., Moya A.;
RT   "Evolutionary convergence and nitrogen metabolism in Blattabacterium strain
RT   Bge, primary endosymbiont of the cockroach Blattella germanica.";
RL   PLoS Genet. 5:E1000721-E1000721(2009).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP001487; ACY40597.1; -; Genomic_DNA.
DR   RefSeq; WP_012841112.1; NC_013454.1.
DR   AlphaFoldDB; D0JBQ9; -.
DR   STRING; 331104.BLBBGE_597; -.
DR   KEGG; bbl:BLBBGE_597; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000002625; 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:ACY40597.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          586..778
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   921 AA;  107226 MW;  47FA2839EC76CCBF CRC64;
     MSDRYSFLNT IHFQDLEFLY NKYKKDPNSI ESSWSAFFHG FDFGKENYKT DRQSINQENH
     KKFLKNENEI DIIHKEFLVF NLIHAYRKRG HFFTPTNPIR ERRKHFPSLD LKNFGLSDKE
     LDISFEAGKL IGLGRTSLRN IIDYLKNIYC GSIGIEYMYI SNPDKIQWIE KWFQKEKLQF
     SAEEKKFFLK KLNEAVAFEN FIHTKFVGQK RFSIEGNESA LPALEEMIEY TSRKYFTEDF
     IIGMSHRGRI NLLSNFFQKN LSQIFSEFQG KEYKEKTFSG DVKYHLGFSK IRKTSQGRYI
     KMNLVPNPSH LESVDAIVEG ITRAKIDIIY NQNSNSEKII PILIHGDAAL AGQGIVYEVI
     QLSRLKGYKT GGTIHIVLNN QIGFTTNYTE GRSSIYCTDI AKIVLSPVLH VNADDVESVI
     RAIHFAVDFR MQYHEDVFID LLGYRKYGHN EGDEPRFTQP SLYKAISKHP NSYNLYKQKL
     EKEGIINSDE IINMEKEYEQ ILNGGYHEAI NIKWNVLNSF LEEEWKNFPI VSNHEDIFHK
     VDTRIPMKKI VDISNQVFSL PKNKKFFRKT ESIFQQRLEM IQLKLVDWSM AEILAYGTLL
     DEGVHIRLSG EDVARGTFSQ RHAIVKTEEE EEIILLNHIR MGQGKMQVYN SPLSEYGVLG
     FDYGYAMYSP HVLTLWEAQF GDFGNGGQII IDQYISSGEN KWKISNGIVL LLPHGYEGQG
     PEHSSARVER YLQLCANNNL FVVNCTTPAN FYHLLRRQMK LKYRKPLIVF TPKSLLRNPK
     CLSTIEDLSE GKFQEILDDP SVIDIHQITR LIFCSGKIYY ELLNKKEALK NDKTALIRIE
     QIYPLKMEKI KELLIKYKNK KEVFWVQEEP ENMGLWSFIL RKLGSIISFN LIAPSESSSP
     STGSYPDFLK IQNKILEKAF F
//