ID A9IIU7_BORPD Unreviewed; 956 AA.
AC A9IIU7;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 71.
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:CAP42171.1};
GN OrderedLocusNames=Bpet1832 {ECO:0000313|EMBL:CAP42171.1};
OS Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Bordetella.
OX NCBI_TaxID=340100 {ECO:0000313|EMBL:CAP42171.1, ECO:0000313|Proteomes:UP000001225};
RN [1] {ECO:0000313|EMBL:CAP42171.1, ECO:0000313|Proteomes:UP000001225}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448
RC {ECO:0000313|Proteomes:UP000001225};
RX PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA Gross R., Guzman C.A., Sebaihia M., Martins Dos Santos V.A., Pieper D.H.,
RA Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA Schneiker-Bekel S., Schulze K., Vorhoelter F.J., Yevsa T., Engle J.T.,
RA Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA Martinez-Arias R.;
RT "The missing link: Bordetella petrii is endowed with both the metabolic
RT versatility of environmental bacteria and virulence traits of pathogenic
RT Bordetellae.";
RL BMC Genomics 9:449-449(2008).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM902716; CAP42171.1; -; Genomic_DNA.
DR AlphaFoldDB; A9IIU7; -.
DR STRING; 94624.Bpet1832; -.
DR KEGG; bpt:Bpet1832; -.
DR eggNOG; COG0567; Bacteria.
DR Proteomes; UP000001225; 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:CAP42171.1};
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; 106532 MW; D541BC85A6A0C3AE CRC64;
MSSESESLSN SYLFGGNAPY VEELYESYLD NPGSVPDNWR EYFDQLQHAP ATDGQESTRD
QAHAPIVQSF AQRARTNGFV QHSVQPDLSM ASKQVSVQSL IAAYRSLGSR WADLDPLKRR
ERPPIPELDP AFYGLTEADL DQTYSATNTY FTTASTMTLR DILKALRDTY CRSIGAEFTH
ISDPAAKRWI QERLEKSFGA ATYTAEEKRH ILQQLTESEG LERFLHTKYV GQKRFSLEGG
ESFIASMDEV VNHAGESGVQ EIVVGMAHRG RLNLLVNIMG KMPGDLFAEF EGKHAEGLTD
GDVKYHNGFS SDLSTRGGPV HLSLAFNPSH LEIVNPVVEG SVRARQERRG DHEGKQVLPV
LVHGDAAFAG QGVVMETLNL AQTRGYGTGG TLHIVINNQI GFTTSDPRDS RSTLYCTDVV
KMIEAPVFHV NGDDPEAVVF ATKLALDYRM QFSHDVVLDI VCFRKLGHNE QDTPSLTQPL
MYKSIGHHPG TRKLYADKLT AQGVLAEGEG DQMVKDYRQL MEDGQRTIEP VLTDYKSKYA
IDWSPFMGAK WTDQADTAVP LAELKRIGER ITTVPEGFTV HPLVNKLLND RRNMAKGEMN
LDWGMGEHLA FATLVASGYA VRITGQDSGR GTFTHRHAVL HDQNRERWND GTYVPLQNVS
DGQAPFTVID SVLSEEAVLG FEYGYSSAEP NTLTIWEAQF GDFVNGAQVV IDQFISSGEA
KWGRQSGLTL MLPHGYEGQG PEHSSGRIER FLQLCADNNI QVVQPTTASQ IFHLLRRQMI
RPFRKPLVIF TPKSLLRNKD AGSPLTELAG GSFRPVIGEL DDSIDASKVK RVLACSGKVY
YDLVNARRER EASHVAIVRV EQLYPFAHKS FEAELRKYGQ ATEVVWVQDE PQNQGPWFYV
QHHLYENMAE GQKLGYAGRP ASASPAVGYL AKHQEQQKAL IEQAFAAKYK GFMLTK
//
