ID   A0A2N5Y4W0_9GAMM        Unreviewed;       947 AA.
AC   A0A2N5Y4W0;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 18.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=CWI75_07690 {ECO:0000313|EMBL:PLW83427.1};
OS   Kineobactrum sediminis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC   Kineobactrum.
OX   NCBI_TaxID=1905677 {ECO:0000313|EMBL:PLW83427.1, ECO:0000313|Proteomes:UP000234845};
RN   [1] {ECO:0000313|Proteomes:UP000234845}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F02 {ECO:0000313|Proteomes:UP000234845};
RA   Du Z.-J., Chang Y.-Q.;
RT   "The draft genome sequence of Chromatocurvus sp. F02.";
RL   Submitted (NOV-2017) 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:PLW83427.1}.
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DR   EMBL; PKLZ01000003; PLW83427.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5Y4W0; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000234845; 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   Reference proteome {ECO:0000313|Proteomes:UP000234845};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          597..790
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   947 AA;  106661 MW;  2C9F29EFD5AB2E81 CRC64;
     MELLRKSSHI AGGNATYVED LYESYLLDPN GVPEQWREYF EKLPRVESPH GTLQDVPHSI
     IRDRFAQISK MRVRTEATVA HDSQATEYER KQVRVVQLVS AYRQRGHQKA SLDPLSLHMR
     DPVPDLDLGF HKLSTADLET VFQTGNMYIG KTDATLGEIV ESLERTYCHT IGAEFMHIVD
     TEQRHWIMQR MESVRSAPNY SDDMRTQLLR SLIKAEGLEK SLASKYPGTK RFGLEGGESL
     IPMLSEMVQR SGSYGAKEIV IGMAHRGRLN VLVNIFGKNP SDLFAEFEGR VVYDKSGDVK
     YHQGFSSNVM TPGGEVHLAL AFNPSHLEIV SPVVEGSVRA RQDRRRDPVG NTVVPIVIHG
     DAAFAGQGVV METFQMSQTR AYKTGGTLHI VLNNQVGFTT SDREDARSTE YCTDIAKMVQ
     APIFHVNADD PQAVHFVTQL AGDFRNTFHR DVVIDLVCYR RRGHNEADEP SVTQPLMYER
     IRKQKTTRDL YAAELIAQGV ITAEEDERLV NGYRESLDRG KPLVSGLVSE PNPSLFVDWT
     PYLGHEWNME YDTSMDLQAL QALAHDINVA PEGFPLQRQV AKILEDRRKM AAGALALNWG
     AAETLAYATL LQAGYPVRLT GQDVGRGTFS HRHAVLHNQK DASRYIPLQH IREDQADFCI
     LDSLLSEEAV LAFEYGYSTT SPTGLVIWEA QFGDFANGAQ VVIDQFITSG EHKWSRLCGL
     TMLLPHGYEG QGPEHSSARL ERFLQLCAEH NIQVCVPTTP AQVYHMLRRQ AIRPVRKPLV
     VMSPKSLLRH KEAVSSLEDL ADGHYYNVLD ETDPIDKQAV ARIILCSGKV YYDLRAARRE
     RDIDNIAIVR LEQLYPFPEA ELLDVLSGYP NITEAVWCQE EPQNQGAWYS SQHHMRRVLF
     SHRTGVYLSY VGREPSAAPA AGYMALHLAQ QEEFINEALA PVVPRQR
//