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
//