ID   Q7VZ18_BORPE            Unreviewed;       956 AA.
AC   Q7VZ18;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 105.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=odhA {ECO:0000313|EMBL:CAE41422.1};
GN   Synonyms=sucA {ECO:0000313|EMBL:CAE41422.1};
GN   OrderedLocusNames=BP1124 {ECO:0000313|EMBL:CAE41422.1};
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE41422.1, ECO:0000313|Proteomes:UP000002676};
RN   [1] {ECO:0000313|Proteomes:UP000002676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC   {ECO:0000313|Proteomes:UP000002676};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
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; BX640414; CAE41422.1; -; Genomic_DNA.
DR   RefSeq; NP_879903.1; NC_002929.2.
DR   RefSeq; WP_003813631.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VZ18; -.
DR   STRING; 257313.BP1124; -.
DR   PaxDb; 257313-BP1124; -.
DR   GeneID; 69601044; -.
DR   KEGG; bpe:BP1124; -.
DR   PATRIC; fig|257313.5.peg.1205; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_4; -.
DR   Proteomes; UP000002676; 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:CAE41422.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002676};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          601..798
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   956 AA;  106472 MW;  2077564C79C67F59 CRC64;
     MSTESESLST SYLFGGNAPY VEELYESYLD NPGSVPDNWR EYFDQLQHSP ATDGQEATRD
     QAHAPIVESF AQRARANAFV QRVAEPDLSV ASKQVSVQSL IAAYRSLGSR WADLDPLKRQ
     ERPAIPELDP AFYGLTEADL DQVYSATNTY FTTASTMTLR DILKALRDTY CRSVGAEFMH
     ISDPAAKRWI QQRLESTFSA PVFSTEEKRH ILQQLTESEG LERFLHTKYV GQKRFSLEGG
     ESFIASMDEV VNHAGESGVQ EIVVGMAHRG RLNLLVNIMG KMPGDLFAEF EGKHAEGLTD
     GDVKYHNGFS SDLSTRGGPV HLSLAFNPSH LEIVNPVVEG SVRARQERRG DGEGKQVLPV
     LVHGDAAFAG QGVVMETLNL AQTRGYGTGG TLHIVINNQI GFTTSDPRDS RSTLYCTDVV
     KMIEAPVFHV NGDDPEAVVF ATRLALDYRM QFRHDVVLDI VCFRKLGHNE QDTPSLTQPL
     MYKRIGHHPG TRKLYADKLT TQGVLAEGDA DQLVKDYRQL MEDGQRTIEP VLTDYKSKYA
     IDWSPFLGAK WTDQADTAVP LAELKRIGER ITTVPEGFTV HPLVAKLLND RRNMAKGEVN
     LDWGMGEHLA FATLVASGYA VRITGQDSGR GTFTHRHAVL HDQNRERWND GFYVPLQNVS
     EGQAPFTVID SVLSEEAVLA FEYGYSSAEP NTLTIWEAQF GDFVNGAQVV IDQFITAGEA
     KWGRQSGLTL MLPHGYEGQG PEHSSGRIER FLQLCADHNI QVVQPTSAAQ IFHLLRRQMI
     RPFRKPLVIF TPKSLLRNKD AGSPLTDLAG GSFRPVIGEV DESIKAASVK RVLACSGKVY
     YDLVNARRER GADHVAIVRV EQLYPFAHKA FETELRKYPK ATEVIWVQDE PQNQGPWFYV
     QHHLYENMAD GQKLGYAGRA ASASPAVGYL AKHQEQQKAL IEQAFAAKYK GFMLTK
//