ID   D9QKF7_BRESC            Unreviewed;       998 AA.
AC   D9QKF7;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   27-MAR-2024, entry version 58.
DE   RecName: Full=2-oxoglutarate dehydrogenase E1 component {ECO:0000256|ARBA:ARBA00013321};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   AltName: Full=Alpha-ketoglutarate dehydrogenase {ECO:0000256|ARBA:ARBA00030680};
GN   OrderedLocusNames=Bresu_0468 {ECO:0000313|EMBL:ADK99782.1};
OS   Brevundimonas subvibrioides (strain ATCC 15264 / DSM 4735 / LMG 14903 /
OS   NBRC 16000 / CB 81) (Caulobacter subvibrioides).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC   Caulobacteraceae; Brevundimonas.
OX   NCBI_TaxID=633149 {ECO:0000313|EMBL:ADK99782.1, ECO:0000313|Proteomes:UP000002696};
RN   [1] {ECO:0000313|Proteomes:UP000002696}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15264 / DSM 4735 / LMG 14903 / NBRC 16000 / CB 81
RC   {ECO:0000313|Proteomes:UP000002696};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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   -!- SUBUNIT: Homodimer. Part of the 2-oxoglutarate dehydrogenase (OGDH)
CC       complex composed of E1 (2-oxoglutarate dehydrogenase), E2
CC       (dihydrolipoamide succinyltransferase) and E3 (dihydrolipoamide
CC       dehydrogenase); the complex contains multiple copies of the three
CC       enzymatic components (E1, E2 and E3). {ECO:0000256|ARBA:ARBA00011301}.
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DR   EMBL; CP002102; ADK99782.1; -; Genomic_DNA.
DR   RefSeq; WP_013267886.1; NC_014375.1.
DR   AlphaFoldDB; D9QKF7; -.
DR   STRING; 633149.Bresu_0468; -.
DR   KEGG; bsb:Bresu_0468; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_5; -.
DR   InParanoid; D9QKF7; -.
DR   OrthoDB; 9759785at2; -.
DR   BioCyc; BSUB633149:G1GM8-466-MONOMER; -.
DR   Proteomes; UP000002696; 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:ADK99782.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002696};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          644..837
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          62..107
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        62..77
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   998 AA;  110567 MW;  66FA8C956EFE4E95 CRC64;
     MADDAGRLNQ VFAETSFLYG SNAAFIEELH DKWAADPSSV SAEWRGFFDQ LRDSAATVQA
     SSAAGSWGRS QATEPTEETG VFDGRWPAPK ADPKAKPAAG APAAPAATGA SAEEVRAAAH
     DSIRVLMLIR SYRVRGHLQA TLDPLGIEAR TNNPELTPEF YGFTEADMDR PIYLDGVLGL
     QTGTIREVLA ILNRTYCGNI GIQFMHIAEP EEKSWLQQRF EGADAFEKNG FTREGKIAIL
     NKLIEAEGFE RFLHKRFPGT KRFGLDGGEA MVPALEQMIK RGGALGVDEI VIGMAHRGRL
     NTLAAVMGKP YRAIFHEFQG GSTVPSDIEG SGDVKYHMGA SSNREFDGNH VHLSLTANPS
     HLEIVNPVVL GKARAKQAFD IREANAGLPE AQWALDRSKV MPLLIHGDAA FAGQGVVAEC
     FALMGLKGYR TGGTMHFVIN NQIGFTTSPR NSRSSPYPSD VALMVQAPIF HVNGDDPEAV
     VFAAKVATEF RQKFKKDVVV DMFCYRRFGH NEGDDPTFTQ PVMYSKIRSL PSTREIYSRR
     LVEEGVLSAA EVDAEIARFE AYLDEQFEAG KSFVADKADW LDGQWKGVGL PDGEERRGDT
     AVAEAKLKDL GHRLTTIPNQ VDIHKTLKRV IDARRATIDK GTDIDWATAE SLAFASLLTE
     GFPVRLSGQD SVRGTFSQRH SGIVDQTTEE RYVPLNNLGG DHQHFEVIDS ALSEEAVLGF
     EYGYALSDPN TLVMWEAQFG DFVNGAQVVI DQFISSGERK WLRMCGLTML LPHGYEGQGP
     EHSSARLERF LQQCAEDNMQ VANCTTPANY FHILRRQMHR PFRKPLIIMT PKSLLRHKKA
     VSTLKDMAEG SSFHRVLHDD AQTRPEVSGI TIKGDKDIRR VVLCSGKVYY DLLDAREKKG
     VNDVYLMRLE QFYPWPIKSL STELARFPNA ELVWCQEEPK NMGGWTFVDP WLELTLEKLD
     VKSKRARYVG RPASASTAAG LMSRHLKELE AFTSEALA
//