ID   A5FKI2_FLAJ1            Unreviewed;       924 AA.
AC   A5FKI2;
DT   12-JUN-2007, integrated into UniProtKB/TrEMBL.
DT   12-JUN-2007, sequence version 1.
DT   27-MAR-2024, entry version 90.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   Name=kgd {ECO:0000313|EMBL:ABQ04288.1};
GN   OrderedLocusNames=Fjoh_1256 {ECO:0000313|EMBL:ABQ04288.1};
OS   Flavobacterium johnsoniae (strain ATCC 17061 / DSM 2064 / JCM 8514 / NBRC
OS   14942 / NCIMB 11054 / UW101) (Cytophaga johnsonae).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=376686 {ECO:0000313|EMBL:ABQ04288.1, ECO:0000313|Proteomes:UP000006694};
RN   [1] {ECO:0000313|EMBL:ABQ04288.1, ECO:0000313|Proteomes:UP000006694}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17061 / DSM 2064 / JCM 8514 / NBRC 14942 / NCIMB 11054 /
RC   UW101 {ECO:0000313|Proteomes:UP000006694};
RX   PubMed=19717629; DOI=10.1128/AEM.01495-09;
RA   McBride M.J., Xie G., Martens E.C., Lapidus A., Henrissat B., Rhodes R.G.,
RA   Goltsman E., Wang W., Xu J., Hunnicutt D.W., Staroscik A.M., Hoover T.R.,
RA   Cheng Y.Q., Stein J.L.;
RT   "Novel features of the polysaccharide-digesting gliding bacterium
RT   Flavobacterium johnsoniae as revealed by genome sequence analysis.";
RL   Appl. Environ. Microbiol. 75:6864-6875(2009).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP000685; ABQ04288.1; -; Genomic_DNA.
DR   RefSeq; WP_012023337.1; NZ_MUGZ01000003.1.
DR   AlphaFoldDB; A5FKI2; -.
DR   STRING; 376686.Fjoh_1256; -.
DR   KEGG; fjo:Fjoh_1256; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000006694; 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:ABQ04288.1};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          585..778
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   924 AA;  104609 MW;  E631F5C992EAF049 CRC64;
     MDRFSFLNAA HTEFFAQLYD QYLVNPDSVE PSWRSFFQGF DFGQTTYNDE NPVQTIVEYV
     TSPNTDYSQV SDKLQKEFNV LKLIDGYRTR GHLFTKTNPV RDRRQSSPTL DIENFGLSTA
     DLSTVFDAAQ TIGMTPSSLE AIVNRLKAIY CQHIGIEYMY IRNPGVVKWI QDKLAVNVNQ
     PNFSTEEKKT ILNKLNEAVS FENFLHTKYV GQKRFSLEGG ESIIPALDAL IEQAAEKGVE
     QFVMGMAHRG RLNVLANIFG KSTQDIFGEF DGKDYDQEYF DGDVKYHLGL TADKKTRSGK
     SININLAPNP SHLETVGAVI EGITRAKQDK YYNDDFSKVL PIAVHGDAAI AGQGILYEII
     QMAQLDGYKT GGTIHIVINN QVGFTTNYLD ARSSTYCTDV AKVTLSPVLH VNADDAEAVV
     HAVSFALDYR MQFGRDVFID LLGYRKYGHN EGDEPRFTQP VLYKIIAKHK NPRDIYAEKL
     LSDGVIDASY VNGLEKQYKS QLEENLEASR KKDLTIITPF MKNEWEGFVQ VTDTQMLQKV
     DTTFAKEGLD SIIKTISTLP EDKKFINKIT KIVTDRKVGY DNNTLDWGTA EALAYGSLLT
     EGFDVRISGQ DVERGTFSHR HAVVKVEDSE EEVILLDAIE NKKGKFGVFN SLLSEYGVLG
     FDYGYALANP KALTIWEAQF GDFSNGAQIM IDQYISCGED KWNNQNGIVL LLPHGYEGQG
     AEHSSARMER YLQLCARHNM YVADCTTPAN FFHLLRRQMK TNFRKPLVVF SPKSLLRDPR
     CVSTVEELAT GSFQETIDDT TVNKKDVKTL VFCTGKFYYD IVAERENNGR KDVAVVRIEQ
     LFPFPVEQIK EIIAKYPNAD DYVWAQEEPK NMGAYSFMLM NFDLVKWRLA SLKAYSAPAS
     GSYTRAKRRH ADAIRMVFDK NLFR
//