ID Q7W5S2_BORPA Unreviewed; 957 AA.
AC Q7W5S2;
DT 01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2003, sequence version 1.
DT 27-MAR-2024, entry version 107.
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:CAE38502.1};
GN Synonyms=sucA {ECO:0000313|EMBL:CAE38502.1};
GN OrderedLocusNames=BPP3217 {ECO:0000313|EMBL:CAE38502.1};
OS Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=257311 {ECO:0000313|EMBL:CAE38502.1, ECO:0000313|Proteomes:UP000001421};
RN [1] {ECO:0000313|Proteomes:UP000001421}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12822 / ATCC BAA-587 / NCTC 13253
RC {ECO:0000313|Proteomes:UP000001421};
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; BX640432; CAE38502.1; -; Genomic_DNA.
DR RefSeq; WP_010928955.1; NC_002928.3.
DR AlphaFoldDB; Q7W5S2; -.
DR GeneID; 69422593; -.
DR KEGG; bpa:BPP3217; -.
DR HOGENOM; CLU_004709_1_0_4; -.
DR Proteomes; UP000001421; 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:CAE38502.1};
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; 106601 MW; F27D2576BF516A32 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 ITTTVPEGFT VHPLVAKLLN DRRNMAKGEV
NLDWGMGEHL AFATLVASGY AVRITGQDSG RGTFTHRHAV LHDQNRERWN DGFYVPLQNV
SEGQAPFTVI DSVLSEEAVL AFEYGYSSVE PNTLTIWEAQ FGDFVNGAQV VIDQFITAGE
AKWGRQSGLT LMLPHGYEGQ GPEHSSGRIE RFLQLCADHN IQVVQPTSAA QIFHLLRRQM
IRPFRKPLVI FTPKSLLRNK DAGSPLTDLA GGSFRPVIGE VDESIKAASV KRVLACSGKV
YYDLVNARRE RGADHVAIVR VEQLYPFAHK AFETELRKYP KATEVIWVQD EPQNQGPWFY
VQHHLYENMA DGQKLGYAGR AASASPAVGY LAKHQEQQKA LIEQAFAAKY KGFMLTK
//
