ID   E1SNL6_FERBD            Unreviewed;       935 AA.
AC   E1SNL6;
DT   30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT   30-NOV-2010, sequence version 1.
DT   27-MAR-2024, entry version 59.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   OrderedLocusNames=Fbal_2487 {ECO:0000313|EMBL:ADN76689.1};
OS   Ferrimonas balearica (strain DSM 9799 / CCM 4581 / KCTC 23876 / PAT).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Ferrimonadaceae; Ferrimonas.
OX   NCBI_TaxID=550540 {ECO:0000313|EMBL:ADN76689.1, ECO:0000313|Proteomes:UP000006683};
RN   [1] {ECO:0000313|EMBL:ADN76689.1, ECO:0000313|Proteomes:UP000006683}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 9799 / CCM 4581 / KCTC 23876 / PAT
RC   {ECO:0000313|Proteomes:UP000006683};
RX   DOI=10.4056/sigs.1161239;
RA   Nolan M., Sikorski J., Davenport K., Lucas S., Glavina Del Rio T., Tice H.,
RA   Cheng J., Goodwin L., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Ovchinnikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA   Chang Y., Jeffries C., Tapia R., Brettin T., Detter J., Han C.,
RA   Yasawong M., Rohde M., Tindall B., Goker M., Woyke T., Bristow J.,
RA   Eisen J., Markowitz V., Hugenholtz P., Kyrpides N., Klenk H., Lapidus A.;
RT   "Complete genome sequence of Ferrimonas balearica type strain (PAT).";
RL   Stand. Genomic Sci. 3:174-182(2010).
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; CP002209; ADN76689.1; -; Genomic_DNA.
DR   RefSeq; WP_013345995.1; NC_014541.1.
DR   AlphaFoldDB; E1SNL6; -.
DR   STRING; 550540.Fbal_2487; -.
DR   GeneID; 67182696; -.
DR   KEGG; fbl:Fbal_2487; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_6; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000006683; 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:ADN76689.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006683};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          593..786
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   935 AA;  104310 MW;  3285D58D4DD022C5 CRC64;
     MQQGSLKAWQ ASSHFAGANA AYIEELYEAY LDDPNAVSEE WQAIFAELPS QGVGTDVAHS
     RIRDYFRATA LDSNRSKTTT VDPEVTEKQV RVLQLINAFR FRGHQNANLD PLGLWQREPV
     AELDLAHHGL TEDDLGREFN TGSYALGNGT MKLGELFNSL KATYCGPIGA EYMHITSTEE
     KRWLQQRLEP VMGQGSYDAD TKKRILAGLN AAEGLEKYLG AKFPGAKRFS LEGGDAMIPM
     MRELIYRAGD QGAKEVVVGM AHRGRLNMLV NILGKKPGDL FDEFAGKHDE ALGSGDVKYH
     QGFSSDFATP GGNVHLALAF NPSHLEIVSP VVMGSVRARM DRRNCETGKL VMPITIHGDS
     AITGQGIVQE TFNMSQTRGF KVGGAIRIVV NNQVGFTTSN PEDTRSTEYC TDIAKMVQAP
     VLHVNADDPE AVAFVAQLAV DFRYEFGRDV VIDLICYRRH GHNEADEPNA TQPLMYQKIK
     KHPTPRKIYA DRLIEQGVMN AEEVTEQINT YREQLDQGEC VVPEWRTMTE HSVDWTPYLG
     HDWDESWDSQ VGLDKLKALA TSICEVPESH KLQSRVAKIY KDREAMAAGD KPLDWGMAET
     LAYATLLDSG YRVRLTGQDS GRGTFFHRHA VLHNQDNATT YMPLRHLGEH QGPIEIFDSV
     LSEAAVLAFE YGYATAEPSG LTMWEAQFGD FANGAQVVID QFLSSGEQKW GRLCGLTLLL
     PHGYEGQGPE HSSARLERFL QLCADHNMQV VVPSTPAQVY HMLRRQVVRP MRRPLVVMSP
     KSLLRHPMAV SSLEELALGD FQNVIGELDE LDPAKVDRVV FCSGKVYFEL LEKRRREELT
     NVALIRIEQL YPFPHAEMAQ VLEAYQHVKE FVWCQEEPQN QGAWYCSQHH FWQAIPAGAN
     LTYAGREASA APACGYVSVH NKQQQALVNA ALGLN
//