ID A0A0H3KEJ0_BURM1 Unreviewed; 954 AA.
AC A0A0H3KEJ0;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 27-MAR-2024, entry version 38.
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:BAG43422.1};
GN OrderedLocusNames=BMULJ_01493 {ECO:0000313|EMBL:BAG43422.1};
OS Burkholderia multivorans (strain ATCC 17616 / 249).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=395019 {ECO:0000313|EMBL:BAG43422.1, ECO:0000313|Proteomes:UP000008815};
RN [1] {ECO:0000313|EMBL:BAG43422.1, ECO:0000313|Proteomes:UP000008815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17616 / 249 {ECO:0000313|Proteomes:UP000008815};
RA Ohtsubo Y., Yamashita A., Kurokawa K., Takami H., Yuhara S., Nishiyama E.,
RA Endo R., Miyazaki R., Ono A., Yano K., Ito M., Sota M., Yuji N.,
RA Hattori M., Tsuda M.;
RT "Complete genome sequence of Burkholderia multivorans ATCC 17616.";
RL Submitted (APR-2007) 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};
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DR EMBL; AP009385; BAG43422.1; -; Genomic_DNA.
DR RefSeq; WP_006414736.1; NC_010804.1.
DR AlphaFoldDB; A0A0H3KEJ0; -.
DR STRING; 395019.BMULJ_01493; -.
DR KEGG; bmj:BMULJ_01493; -.
DR eggNOG; COG0567; Bacteria.
DR HOGENOM; CLU_004709_1_0_4; -.
DR Proteomes; UP000008815; Chromosome 1.
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:BAG43422.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008815};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT DOMAIN 600..797
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 954 AA; 106798 MW; 519351AF573A2EBE CRC64;
MSDVMKQFQL NSYLFGGNAS YVEEQYEAYL DNPASVPENW REYFDALQNV PATDGSNASD
VAHYPIVESF AQRAKANAFI PRESGTNLAT ARKQVHVQSL ISAYRFLGSQ WANLDPLKRR
ERPAIPELEP AFYDFSEADL DQTYSASNLY FGFDQASLRD IVKGLRDTYC GTIGAEFMYI
SDPEQKRWWQ ERLESIRATP NFSADKKKHI LNRLTAAEGL ERYLHTKYVG QKRFSLEGGE
SFIAAMDEVV QHAGKKGVQE IVIGMAHRGR LNVLVNTLGK MPADLFAEFE GKHVDDLPAG
DVKYHKGFSS DVSTEGGPVH LSLAFNPSHL EIVNPVVEGS AKARMDRRGD EDGAQVLPVQ
IHGDAAFAGQ GVVMETLNLA QTRGYGTHGT LHIVINNQIG FTTSDPRDAR STLYCTDVVK
MIEAPVLHVN GDDPEAVVLA TQIAIDYRMQ FHKDVVIDIV CFRKLGHNEQ DTPAVTQPLM
YKKIAQHPGT RALYAEKLVQ QGVITAEDAE AYVKAYRKAM DDGHHTVDPV LSNYKSKYAV
DWVPFLNRKW TDAADTAVPL AELKRLGERI TTVPENFKVH PLVERVINDR RNMARGDQPL
DWGMAEHLAF ASLVASGYAV RLTGQDSGRG TFTHRHAVLH DQNRERWNDG TYVPLQNIAE
GQAKFTVIDS VLSEEAVLGF EYGYSTAEPN TLVLWEAQFG DFVNGAQVVI DQFISSGEVK
WGRVSGLTML LPHGYEGQGP EHSSTRIERF LQLCADHNMQ VVQPTTPAQI FHLLRRQMIR
LFRKPLIVAT PKSLLRHKEA VSDLSELAKG SFQPVLGEID GGIDAKKVKR VLVCSGRVYY
DLVAHRRETK ANDVAIIRIE QLYPFAHKQF EAEMKKYENA TEVVWVQDEP QNQGPWFYVE
HHLKEGMKEG QKLAYSGRPA SASPAVGYYA KHYEQQKALV EGAFGRLKSA SIAK
//
