ID   A0A261U6Z8_9BORD        Unreviewed;       957 AA.
AC   A0A261U6Z8;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=CAL20_08095 {ECO:0000313|EMBL:OZI57361.1};
OS   Bordetella genomosp. 4.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=463044 {ECO:0000313|EMBL:OZI57361.1, ECO:0000313|Proteomes:UP000216885};
RN   [1] {ECO:0000313|EMBL:OZI57361.1, ECO:0000313|Proteomes:UP000216885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU9919 {ECO:0000313|EMBL:OZI57361.1,
RC   ECO:0000313|Proteomes:UP000216885};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) 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};
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:OZI57361.1}.
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DR   EMBL; NEVQ01000012; OZI57361.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261U6Z8; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000216885; 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   Reference proteome {ECO:0000313|Proteomes:UP000216885};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          602..799
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   957 AA;  106740 MW;  D4BAA3235D1A09DB CRC64;
     MSSESESLST SYLFGGNAPY VEELYEAYLD NPGSVPDNWR EYFDQLQHSP ATDGQETTRD
     RAHAPIVESF AQRARNNGFV QQVSAQPDLS IASKQVSVQS LIGAYRSLGS RWADLDPLKR
     QERPPIPELD PSFYGLTEAD LDQTYSATNT YFTTASTMTL RDILKALRDT YCRSIGAEYT
     HISDPAAKRW IQERLEKTFG AASYSNEEKR HILQQLTESE GLERFLHTKY VGQKRFSLEG
     GESFIASMDE VVNHAGESGV QEIVVGMAHR GRLNLLVNIM GKMPGDLFAE FEGKHAEGLT
     DGDVKYHNGF SSDLSTRGGP VHLSLAFNPS HLEIVNPVVE GSARARQERR GDPEGKQVLP
     VLVHGDAAFA GQGVVMETLN LAQTRGYGTG GTLHIVINNQ IGFTTSDPRD TRSTLYCTDV
     VKMIEAPVFH VNGDDPEAVV FATKLALDYR MQFHHDVVLD IVCFRKLGHN EQDTPALTQP
     LMYKRIGHHP GTRKLYADKL TSQGVLAEGE ADQMVKDYRQ LMEDGQRTIE PVLTDYKSKY
     AIDWSPFLGA KWTDQADTAV PLAELKRIGE RITTVPDSFT PHPLVKKLLT ERRKMAEGEQ
     NLDWGMGEHL AFATLVASGY AVRITGQDSG RGTFTHRHAV LHDQNRERWN DGTYVPLQNV
     SDGQAPFTVI DSVLSEEAVL GFEYGYSCAE PNTLTIWEAQ FGDFVNGAQV VIDQFISSGE
     AKWGRQSGLT LMLPHGYEGQ GPEHSSGRIE RFLQLCADNN IQVVQPTTAS QIFHLLRRQM
     IRPFRKPLVI FTPKSLLRNK DAGSPLTELA GGSFRPVIGE LDDTIDASKV KRVLVCSGKV
     YYDLVNARTE RDAKHVAIVR IEQLYPFAHK AFEAELRKYA NATEVVWVQD EPQNQGPWFY
     VQHHLYENMA DGQKLGYAGR PASASPAVGY LAKHQEQQKA LVEQAFAAKY KGFMLTK
//