ID   A0A0A6XYV4_9FLAO        Unreviewed;       812 AA.
AC   A0A0A6XYV4;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
DE   Flags: Fragment;
GN   ORFNames=HMPREF9074_09484 {ECO:0000313|EMBL:KHE67830.1};
OS   Capnocytophaga sp. oral taxon 329 str. F0087.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Capnocytophaga.
OX   NCBI_TaxID=706436 {ECO:0000313|EMBL:KHE67830.1, ECO:0000313|Proteomes:UP000030579};
RN   [1] {ECO:0000313|EMBL:KHE67830.1, ECO:0000313|Proteomes:UP000030579}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0087 {ECO:0000313|EMBL:KHE67830.1,
RC   ECO:0000313|Proteomes:UP000030579};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; KN390084; KHE67830.1; -; Genomic_DNA.
DR   RefSeq; WP_034540957.1; NZ_KN390084.1.
DR   AlphaFoldDB; A0A0A6XYV4; -.
DR   STRING; 706436.HMPREF9074_09484; -.
DR   eggNOG; COG0567; Bacteria.
DR   HOGENOM; CLU_004709_1_0_10; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000030579; 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; 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; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          587..784
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   NON_TER         812
FT                   /evidence="ECO:0000313|EMBL:KHE67830.1"
SQ   SEQUENCE   812 AA;  91952 MW;  BB00F34F27A781FB CRC64;
     MDKYSFLNAA STAYFGDLYD KYLENPDAIE PSWRAFFQGF DFAQEQYGAP LQEAVPVMVQ
     QVVSNEANKP SEKIEKEFKV LNLINAYRTY GHLLTQINPL AAREPQLIDL SIERYGLSTA
     DLDIVFDSAK EIGLSPTSLR QIVSTLQQLF CRSVGVEYQY IRESSVRQWI DQHLQKNNNI
     TPFSKEDKIR LLRKLNEATS FENFLHTKYV GQKRFSLEGN DALVAGLDFM VEAAAEKGVT
     HLVLGMAHRG RLNVLANVFG KNPQDIFSEF DGKDYEMDDW FDGDVKYHLG ITAERTSRSG
     KKIDMNLVPN PSHLETVAAV VEGITRAKQD RYCKDNPLKA LPIVIHGDAA VCGQGIVYET
     VQMCGLRGFK TGGTIHIVVN NQVGFTTNYT DSRSSIYATD IAKVNDSPVL HVNADDAEAV
     VHTFLFALDF RQAFGKDVFI DLIGYRKYGH NEGDEPRFSQ PKMYKLIGKH DNPRNIYAQK
     LITEGLIQQS LVTEMENEYK ALLDAHLETS RKEPLTVIKP FMQTEWQGFK IASPAEMLQS
     VDTTINKETL TKIAEVLTEM PADKNFISKV KKVVADRKEA FFQNNHIDWG MAELLAYGSL
     LTEGYEVRLT GEDVQRGTFS HRHAVLKTED TEEEVCFLQD LKYKKSMAKG DFHIYNSLLS
     EYGVLGYEYG YALASPYTLT IWEAQFGDFS NGAQIMLDQY ISCGEDKWKV QDGLVMLLPH
     GYEGQGAEHS SARVERYLQL CAENNMYVAN CTTPANFFHL LRRQMKTTFR KPLVVFTPKS
     LLRHPQVISS LEELAEGQFR EVITDPIADA NK
//