ID   A0A0H3HNK5_BURP2        Unreviewed;       954 AA.
AC   A0A0H3HNK5;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   27-MAR-2024, entry version 26.
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:AFI66495.1};
GN   OrderedLocusNames=BP1026B_I1875 {ECO:0000313|EMBL:AFI66495.1};
OS   Burkholderia pseudomallei (strain 1026b).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=884204 {ECO:0000313|EMBL:AFI66495.1, ECO:0000313|Proteomes:UP000010087};
RN   [1] {ECO:0000313|EMBL:AFI66495.1, ECO:0000313|Proteomes:UP000010087}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1026b {ECO:0000313|EMBL:AFI66495.1,
RC   ECO:0000313|Proteomes:UP000010087};
RX   PubMed=22615773; DOI=10.1371/journal.pone.0036507;
RA   Hayden H.S., Lim R., Brittnacher M.J., Sims E.H., Ramage E.R., Fong C.,
RA   Wu Z., Crist E., Chang J., Zhou Y., Radey M., Rohmer L., Haugen E.,
RA   Gillett W., Wuthiekanun V., Peacock S.J., Kaul R., Miller S.I., Manoil C.,
RA   Jacobs M.A.;
RT   "Evolution of Burkholderia pseudomallei in recurrent melioidosis.";
RL   PLoS ONE 7:E36507-E36507(2012).
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; CP002833; AFI66495.1; -; Genomic_DNA.
DR   RefSeq; WP_004526855.1; NZ_CP004379.1.
DR   AlphaFoldDB; A0A0H3HNK5; -.
DR   GeneID; 56526277; -.
DR   KEGG; bpz:BP1026B_I1875; -.
DR   PATRIC; fig|884204.3.peg.2078; -.
DR   Proteomes; UP000010087; 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   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;  106451 MW;  12CDC28BDBD06295 CRC64;
     MSDVMKQFQL NSYLFGGNAS YVEELYEAYL DNPASVPDNW REYFDALQNV PATDGSNASD
     VAHNPIVESF AQRAKANAFI PRESGGNLAT ARKQVHVQSL ISAYRFLGSQ WANLDPLKRR
     ERPAIPELEP AFYDFSEADL DQTFSASNLY FGFEQASLRD IVKGLRDTYC GTIGAEFMYI
     SDPEQKRWWQ ERLESTRATP NFSADKKKHI LNRLTAGEGL ERYLHTKYVG QKRFSLEGGE
     SFIAAMDEVV QHAGSKGVQE IVIGMAHRGR LNVLVNTLGK MPADLFAEFE GKHVDDLPAG
     DVKYHKGFSS DIATEGGPVH LSLAFNPSHL EIVNPVVEGS AKARMDRRGD ADGLQVLPVQ
     IHGDAAFAGQ GVVMETLNLA QTRGYGTHGT LHIVINNQIG FTTSDPRDAR STLYCTDVVK
     MIEAPVLHVN GDDPEAVVLA TQIAIDYRMQ FHKDVVIDIV CFRKLGHNEQ DTPAVTQPLM
     YKKIAQHPGT RALYAEKLVQ QGVISADDAD GFVKAYRKAM DDGHHTVDPV LSNYKSKYAV
     DWMPFLNRKW TDAADTAVPL AELKRLGERI TTVPENFKVH PLVERVINDR RNMARGDQPL
     DWGMGEHLAY ASLVASGYAV RLTGQDSGRG TFTHRHAVLH DQNRERWNDG TYVPLQNVSE
     GQAKFNVIDS VLSEEAVLGF EYGYSTAEPN TLVLWEAQFG DFANGAQVVI DQFISSGEVK
     WGRVSGLTML LPHGYEGQGP EHSSARIERY LQLCAEHNMQ VVQPTTPAQI FHLLRRQMIR
     LFRKPLIVAT PKSLLRHKEA VSDLSELAKG SFQPVLGEVD GGIDAKKVKR VIACSGRVYY
     DLVAHRREAK ANDVAIVRIE QLYPFAHKQF EAEMKKYENA TEVVWVQDEP QNQGPWFYVE
     HHLKEGMKEG QKLAYSGRPA SASPAVGYYA KHYEQQKALV EGAFGRLKSA SIAK
//