ID   A0A495E994_9FLAO        Unreviewed;       658 AA.
AC   A0A495E994;
DT   05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT   05-JUN-2019, sequence version 1.
DT   22-FEB-2023, entry version 11.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:RKR13149.1};
GN   ORFNames=CLV91_1864 {ECO:0000313|EMBL:RKR13149.1};
OS   Maribacter vaceletii.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Maribacter.
OX   NCBI_TaxID=1206816 {ECO:0000313|EMBL:RKR13149.1, ECO:0000313|Proteomes:UP000269412};
RN   [1] {ECO:0000313|EMBL:RKR13149.1, ECO:0000313|Proteomes:UP000269412}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 25230 {ECO:0000313|EMBL:RKR13149.1,
RC   ECO:0000313|Proteomes:UP000269412};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (OCT-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:RKR13149.1}.
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DR   EMBL; RBIQ01000008; RKR13149.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A495E994; -.
DR   OrthoDB; 9771835at2; -.
DR   Proteomes; UP000269412; Unassembled WGS sequence.
DR   GO; GO:0016624; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, disulfide as acceptor; IEA:InterPro.
DR   CDD; cd02000; TPP_E1_PDC_ADC_BCADC; 1.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR001017; DH_E1.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR009014; Transketo_C/PFOR_II.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033248; Transketolase_C.
DR   PANTHER; PTHR42980:SF1; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR42980; 2-OXOISOVALERATE DEHYDROGENASE SUBUNIT BETA-RELATED; 1.
DR   Pfam; PF00676; E1_dh; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   SMART; SM00861; Transket_pyr; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000269412}.
FT   DOMAIN          341..514
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   658 AA;  73818 MW;  1635B33AEAB75F93 CRC64;
     MNYSKYQISK EMHLQLYTAM LKPRMIEEKM LVLLRQGKIS KWFSGIGQEA ISVGVTSALK
     DNEYILPMHR NLGVFTTRNV PLDKLFAQWQ GKQYGFTKGR DRSFHFGSQA HNIIGMISHL
     GPQLGVADGI ALAHKLKNKK LVTAVFSGEG GTSEGDFHEA LNLAAVWDLP VLFCVENNGY
     AISTPTNEQF KCKSIADKGI GYGIESYSIN GNNILKVYKK VKKLAKSMRK NPRPILIEFR
     TFRVRGHEEA SGTKYVPKKI LKKWKAKDPL ENYENYLINK NILSKENKRL IKNKIDNELK
     LNTSSFNAME DSEYSIKKEL ADVFKKHYYQ DIPQGAIVKN IRFVDAISEG LKQSMEIHDN
     LIIMGQDIAE YGGVFKITEG FVEKFGKNRI RNTPICESAI ISAAMGLSIN GMKAMVEMQF
     ADFASSGFNS IVNYLAKSHY RWGQNADVVI RMPCGGGISA GPFHSQTNEA WFTKTPGLKV
     VYPAFPIDAK GLLATAINDP NPVLFFEHKA LYRTINENVP ADYYTTPFGK ASFIESGEDI
     TVVSYGLGVH WAIETLNNNS DINADLIDLR TLHPLDIETV YTSVKKTGRL IILQEDSLFG
     SISSDISALV TENCFDYLDA PIKRVASVET PIPFAAHLEE NYLGKSRFET ALLELLRY
//