ID   A0A069PWH1_9BURK        Unreviewed;       944 AA.
AC   A0A069PWH1;
DT   01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=sucA {ECO:0000313|EMBL:KDR41706.1};
GN   ORFNames=BG61_15630 {ECO:0000313|EMBL:KDR41706.1};
OS   Caballeronia glathei.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=60547 {ECO:0000313|EMBL:KDR41706.1, ECO:0000313|Proteomes:UP000027466};
RN   [1] {ECO:0000313|EMBL:KDR41706.1, ECO:0000313|Proteomes:UP000027466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 50014 {ECO:0000313|EMBL:KDR41706.1,
RC   ECO:0000313|Proteomes:UP000027466};
RA   Liu X.Y., Li C.X., Xu J.H.;
RT   "Draft Genome Sequences of Four Burkholderia Strains.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KDR41706.1}.
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DR   EMBL; JFHC01000024; KDR41706.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A069PWH1; -.
DR   STRING; 60547.GCA_000751215_04994; -.
DR   Proteomes; UP000027466; Unassembled WGS sequence.
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:KDR41706.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027466};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          597..794
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   944 AA;  103098 MW;  1DB2794C9F0DF5F3 CRC64;
     MMLMQKRQSS FLFGGNAPYV EEQYELYLAD PASVPDGWRA YFDALRETPA SDGSDRDDEP
     HAPVVSTFVD LGKRSPASAM TLDDGLAIAR KQVAVQSLIA AFRMVGTRKA KLDPLLWTSP
     HAPVELLPTF YGLSSADMST RFSTADTFLF EDDATLREIV SALEQTYCGT LGAEFMHLSD
     AGERRWWQMR LESTRARPSF SVAEKHRILE RLTAAEGLEK YLHTRYVGQK RFSLEGAESL
     IVLLDELVRY GASKKVSTVV MGMAHRGRLN VLVNIAGKPL RALFDEFDGK NGDDLPAGDV
     KYHKGFSSVT QTSDGPVDVV LAFNPSHLEI VNPVVQGMAR AKGEVSGAGD GSDVLPVEIH
     GDAAMSGQGV VMETLSLSYT RGHGTGGTVH IVVNNQIGFT TSDPRDTRSS FYCTDIAKMI
     EAPVLHVNAD DPEAVAMAVR LALDYRTAFR RSVVIDLVCF RKHGHQEQDT PNVTQPLMYR
     SIAGHPGART VYAQRLIQEG AVSTGQVEDY VNACRDGLER ARESEAPAAS GRQHDIPAWP
     KFLEDYSGPV IYGPPLPAQV RALAQQISTV PDGYELHPLV GKMMAARREM AAGTKPIDWG
     MGEHLAFASL LGAGVDVRLS GQDSARGTFN HRHAVLHNQK RTSRSDGVYI PLDHVDKARG
     RFAVTNSILS EAAVLAFEYG YSTVNRNALV VWEAQFGDFA NGAQVVIDQF IAAGAAKWGQ
     LSGLTLFLPH GQEGQGPEHA SARLERYLQL CAQDNMRVCQ PTTPAQLFHL LRMQAAVFDR
     RPLVVMTPKS LLRHPEAVST LDDLAKGAFR EILGDTQVEA SRASGVERVI ACSGKVYFDL
     LAHRRTSGGA DIPLIRVEQL YPFPSRQLAA EFARYPNLKT VVWCQEESRN QGAWGAIEPQ
     LREILPSAAQ LQYAGSPASA STAPGYHSAH AARQAALISD AFAM
//