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
//