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Database: UniProt
Entry: A0A368MXI1_9FLAO
LinkDB: A0A368MXI1_9FLAO
Original site: A0A368MXI1_9FLAO 
ID   A0A368MXI1_9FLAO        Unreviewed;       929 AA.
AC   A0A368MXI1;
DT   07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT   07-NOV-2018, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   RecName: Full=oxoglutarate dehydrogenase (succinyl-transferring) {ECO:0000256|ARBA:ARBA00012280};
DE            EC=1.2.4.2 {ECO:0000256|ARBA:ARBA00012280};
GN   ORFNames=DQ356_07335 {ECO:0000313|EMBL:RCU42630.1};
OS   Chryseobacterium lacus.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=2058346 {ECO:0000313|EMBL:RCU42630.1, ECO:0000313|Proteomes:UP000252172};
RN   [1] {ECO:0000313|EMBL:RCU42630.1, ECO:0000313|Proteomes:UP000252172}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YLOS41 {ECO:0000313|EMBL:RCU42630.1,
RC   ECO:0000313|Proteomes:UP000252172};
RA   Li C.-M.;
RT   "Chryseobacterium lacus sp. nov., isolated from lake water.";
RL   Submitted (JUL-2018) 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:RCU42630.1}.
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DR   EMBL; QPIE01000005; RCU42630.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A368MXI1; -.
DR   OrthoDB; 9759785at2; -.
DR   Proteomes; UP000252172; 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   ECO:0000313|EMBL:RCU42630.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000252172};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052}.
FT   DOMAIN          585..776
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   929 AA;  105023 MW;  D0CA34C7D606B9F1 CRC64;
     MDRFSFLNAA HSQLIEDLYQ QYKKYPDSLE PSWKAFFQGF EFAQEDYGDQ DSSSASVVQY
     AAQTENSKEI SENVKKEFKV LNLIDAYRSR GHMFTNTNPI RERRHYEPTL DIENFGLTEE
     DLNQTFNSAT EIGIETAATL KEIIARLEKV YCGSIGVEYM HIHDVSEKIW IRKWLQSSEN
     QAVLTEEEKI EILHKLNQAV AFENYLHTKF VGQKRFSLEG GESLIPALDQ LITRSSQLGV
     DEVVLGMAHR GRLNVLTNIF GKSYKAIFSE FEGKEFEEDV FSGDVKYHLG SSKKIKTASG
     EEVSINLTPN PSHLETVAAL VEGICRAKVD DKYKDFKKVL PIIIHGDGAI AGQGIVYEVA
     QMMNLEGYRT GGSVHIVINN QVSFTTNFHD ARSSVYCTDV AKVTGSPVMH VNADDVESVV
     HAIRFAAEFR AEFGKDVYID LLGYRKYGHN EGDEPRFTQP NLYKIISKHP NPREIYKDLL
     KKENVVSDDK LKAMEAEFKA LLDKDFDASK EIQKNTMDVF MGDDWKDFPL CSKGALQENM
     DTSFDINKLK ELAVKMSTLP ADKKFINKVS RLFEQRLKMI DANTIDWALG EWLAYASLLS
     EGKNIRISGE DVERGTFSHR HAIVKTEDTE EEYIPLRHIS ESRFDIYNSH LSEYGVLGFD
     YGYAMASPNT LTIWEAQFGD FVNGAQIIVD QYLAAAEEKW KIQNGLVMLL PHGSEGQGAE
     HSSARLERFL GLCANENMIV ANCTTPANFF HILRRQLAFG FRKPLVVMSP KSLLRHPKVI
     STFEDLAENS FQPIIDDATA DASKVSKLVL CSGKIYYELL AKKEKLGAED VALVRIEQLY
     PLHAESLEGI LTKYSGRKEI IWAQEEPENM GAWSYILRNF RDTGIQVVAP VPSGAPAPGS
     HKMFERIQNG VINRVFDCDD EPESRPVTA
//
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