ID   F0RC09_CELLC            Unreviewed;       922 AA.
AC   F0RC09;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2011, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Celly_1820 {ECO:0000313|EMBL:ADY29643.1};
OS   Cellulophaga lytica (strain ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 /
OS   NCIMB 1423 / VKM B-1433 / Cy l20).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Cellulophaga.
OX   NCBI_TaxID=867900 {ECO:0000313|EMBL:ADY29643.1, ECO:0000313|Proteomes:UP000007487};
RN   [1] {ECO:0000313|EMBL:ADY29643.1, ECO:0000313|Proteomes:UP000007487}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23178 / DSM 7489 / JCM 8516 / NBRC 14961 / NCIMB 1423 /
RC   VKM B-1433 / Cy l20 {ECO:0000313|Proteomes:UP000007487};
RX   PubMed=21677859; DOI=10.4056/sigs.1774329;
RA   Pati A., Abt B., Teshima H., Nolan M., Lapidus A., Lucas S., Hammon N.,
RA   Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA   Liolios K., Pagani I., Mavromatis K., Ovchinikova G., Chen A.,
RA   Palaniappan K., Land M., Hauser L., Jeffries C.D., Detter J.C.,
RA   Brambilla E.M., Kannan K.P., Rohde M., Spring S., Goker M., Woyke T.,
RA   Bristow J., Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C.,
RA   Klenk H.P., Ivanova N.;
RT   "Complete genome sequence of Cellulophaga lytica type strain (LIM- 21).";
RL   Stand. Genomic Sci. 4:221-232(2011).
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; CP002534; ADY29643.1; -; Genomic_DNA.
DR   RefSeq; WP_013621388.1; NC_015167.1.
DR   AlphaFoldDB; F0RC09; -.
DR   STRING; 867900.Celly_1820; -.
DR   KEGG; cly:Celly_1820; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000007487; 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:ADY29643.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007487};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          578..771
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   922 AA;  105372 MW;  8F6C8DF971067824 CRC64;
     MDKYSFLNAA HTSFFATLYD KYLISPDSVE PSWRAFFQGF DFGQETAQEE FSENGPAIEA
     AMPQSLQKEF KVIKLIDGYR SRGHLFTKTN PVRERRKYSP TLELDNFGLS SEDLNTVFTA
     GEILGIGAVS LEEIIKHLKS IYCDAIGVEY MYIRKPERVE WIQNWLNVND NHPKFNADRK
     KHILKKLNQA VSFESFLHTK YVGQKRFSIE GNESLIPALD AVVERAAEMG VEQFVMGMAH
     RGRLNVLTNI FGKAAKDIFS EFDGKDYEQE IFDGDVKYHL GWTSERKASN GNKIKMNIAP
     NPSHLETVGA VVEGIARVKQ DAHFPEDFSK VLPIVVHGDA AIAGQGLVYE VVQMANLDGY
     KTNGTIHIVV NNQIGFTTNY LDARSSTYCT DVAKVTLSPV LHVNADDAEA VVHASLFALE
     YRMRFNRDVF IDLLGYRKYG HNEGDEPRFT QPKLYKAISK HNNSRDIYAE RLLAEGVIEK
     GFVKELENEY KASLEEELED SRKEDKTVIT PFMADEWSGF ASVREWEMME AVDTTYDKDK
     LTEIAKVITE LPSDKKFLRK VEKLVKDRKK MFFETNKLDW AMGELLAYGT LLQEGFGVRM
     SGQDVERGTF SHRHAVMKVE ESEEEIILLN HLSEEQARFQ IYNSLLSEYG VVGFDYGYAM
     ASPKTLTIWE AQFGDFSNGA QIMLDQYISA AEDKWKLQNG LVMLLPHGYE GQGAEHSSAR
     MERYLQLCAR DNMYIADVST PAQMFHILRR QMKVNFRKPL VIFTPKSLLR HPKAVSTIDE
     LANGTFQEVL DDTTADVSKV KSLVFCTGKF YYDLLAEKEE QNREDVALVR VEQLFPLPTE
     KITEIIGRYT NADDIVWAQE EPRNMGAWSH IMMHYKDANK LRVASRRFYA SPAAGSAVRS
     KRRHQQVIDY VFDKTKDNMT KR
//