ID   A0A1B3LHX7_9PROT        Unreviewed;       939 AA.
AC   A0A1B3LHX7;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
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:AOF80455.1};
GN   ORFNames=BSY238_303 {ECO:0000313|EMBL:AOF80455.1};
OS   Methyloversatilis sp. RAC08.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Sterolibacteriaceae; Methyloversatilis.
OX   NCBI_TaxID=1842540 {ECO:0000313|EMBL:AOF80455.1, ECO:0000313|Proteomes:UP000094168};
RN   [1] {ECO:0000313|Proteomes:UP000094168}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC08 {ECO:0000313|Proteomes:UP000094168};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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; CP016448; AOF80455.1; -; Genomic_DNA.
DR   RefSeq; WP_069037591.1; NZ_CP016448.1.
DR   AlphaFoldDB; A0A1B3LHX7; -.
DR   STRING; 1842540.BSY238_303; -.
DR   KEGG; metr:BSY238_303; -.
DR   PATRIC; fig|1842540.3.peg.304; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000094168; 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:AOF80455.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094168};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          590..787
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   939 AA;  104862 MW;  D01BA6C40320B87E CRC64;
     MMQMLSHSYL FGGNAPFVEE LYESYLANPG SVPDAWRSYF ESLQHLPGAA ADVAHAPVVA
     SFAELAKRGP TRSAGPAADD KRQVGVLQMI NAYRFLGNRW AQLDPLKRAE RPDISELEPS
     HYGFTEADLG DVFSTGSFRF PPDDRASLRE ILEAVRQVYC GSVGAEYMYM TDIAHKRWIQ
     ARLEPMRGNY GYSVEDRKRF LERVTAAETM ERYLHTKYVG QKRFSLEGGE STIVAMDELV
     RVAAAQGAQE IVIGMAHRGR LNVLVNTLGK APSMLFSEFE GKAASDLSAG DVKYHMGFSS
     DVNTPSGPVH LTLAFNPSHL EIVNPVVVGS VYARQRRRGD KSGTQVIPVI LHGDAAVAGQ
     GVNQEMLNFS QTRGYGVGGT VHIIVNNQIG FTTSDPRDYR SSLYCTDIFK MVEAPIFHVN
     GDDPEAVAYV TRMAMEFRAE FKKDVVIDII CYRKLGHNEQ DEPMVTQPLM YKKIAAHPGT
     RKIYADRLIS QAVIGEQEPE QMIADYRAAL DEGRLAQDPV LTNHQRRFAV DWTPFLKQPY
     TDECDTRVPK DELARLGKRL TTVPDGFALH SRVQKIIDDR AAMAQGTQPV DWGMGENLAY
     ATLLVEGYGV RVSGEDVGRG TFFHRHAVLH DQRREKWDSG NYMPLQHLQE DQAPCVVIDS
     VLSEEAVLAF DYGYATTEPN ELVVWEAQFG DFANGAQVVF DQFIASGEAK WGRLCGLAMM
     LPHGFEGQGP EHSSARIERY MQLSAENNWQ VTIPSTPAQI FHLLRRQMLR KVRKPLVIIT
     PKSLLRHKDA VSSLDELANG RFQPVIPEVD ALDDKKVERI IMCSGKIYYE LLAHRRANDI
     KNVAIVRLEQ PYPFPSAEVS AQVARYPKAK GITWVQEEPR NQGMWYWLIS RQHLGKAVGD
     MKLELVSRPA AASPAVGYAA KHQAQQKAVI EAAFAGVGR
//