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
//
