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Database: UniProt
Entry: A0A257K1H4_9FLAO
LinkDB: A0A257K1H4_9FLAO
Original site: A0A257K1H4_9FLAO 
ID   A0A257K1H4_9FLAO        Unreviewed;       928 AA.
AC   A0A257K1H4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 15.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=CFE23_06480 {ECO:0000313|EMBL:OYU81131.1};
OS   Flavobacterium sp. BFFFF1.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Flavobacterium.
OX   NCBI_TaxID=2015557 {ECO:0000313|EMBL:OYU81131.1, ECO:0000313|Proteomes:UP000216055};
RN   [1] {ECO:0000313|EMBL:OYU81131.1, ECO:0000313|Proteomes:UP000216055}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BFFFF1 {ECO:0000313|EMBL:OYU81131.1};
RA   Kojadinovic M., Villain A., Puppo C., Fon Sing S., Prioretti L., Hubert P.,
RA   Gregori G., Zhang Y., Sassi J.-F., Claverie J.-M., Blanc G., Gontero B.;
RT   "A metagenomic investigation of the 'star' freshwater diatom Asterionella
RT   formosa and its bacterial cohort.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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:OYU81131.1}.
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DR   EMBL; NKJE01000007; OYU81131.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A257K1H4; -.
DR   Proteomes; UP000216055; 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   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          589..782
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   928 AA;  104791 MW;  BA8C9E280AF0784A CRC64;
     MDRFSFLNAA HTEFFADLYD QYLENPDSVE PSWRSFLQGF DFGMTTYNDE YPVGVPASEI
     ANAAATQDVS QISEKLQKEF NVLKLIDAYR TRGHLFTKTN PVRERRIWSP TLDIANFGLS
     DADLNTVFDA AKAMKLEPCT LTEILGHLKN IYCESIGVEY MYIRKPEVIQ WIQDKIGYND
     NIPKFNADQK KNILEKLNEA VSFENFLHTK YVGQKRFSLE GGESIIPGLD ALIEAAAEKG
     VEQFVMGMAH RGRLNVLANI FGKSTQDIFS EFDGKDYDDD ALFDGDVKYH LGLTSDRKTK
     SGKSININLA PNPSHLETVG AVIEGITRAK QDRYFPDDFS KVLPIALHGD AAVAGQGIVY
     EIVQMAQLDG YRTGGTIHIV INNQVGFTTN YLDARSSTYC TDVAKVTLSP VLHVNADDTE
     AVVHAMLFAL DYRMQFGSDV FIDLLGYRKY GHNEGDEPRF TQPKLYKIIA RHKNPRDIYA
     ERLLAEGVID STFVKGLEDT YKANLEENLE ASRKKDLTII TPFMQNEWQG FKQADQAEML
     QNTDTTFPKE TLTGIAKVIT ELPSDKKFIS KIQKLINDRK TMYFETDKLD WAMAELLAYG
     SLLTEGYDVR ISGQDVERGT FSHRHAVVKV EDSEEEVILL QTLPNAKGKF NIFNSLLSEY
     GVVGFDYGYA LASPKTLTIW EAQFGDFSNG AQIMLDQYIS AAEDKWNNQN GLVMLLPHGY
     EGQGAEHSSA RMERYLQMCA NENMFVADCT TPANFFHLLR RQMKTTYRKP LIVFTPKSLL
     RHPLVVSTAD EFATGTFRET LDDTTVNKAD VKSLVFCTGK FYYDLLAERE ANGRKDVALV
     RIEQLFPLPV EQLKAIIASY PNADDYVWAQ EEPRNMGAYS YMLMNFKEVK LRVASLKAYS
     APAAGSYARS KKRHAAAIAM VFDKNLFN
//
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