ID   A0A1I2YYF0_9SPHI        Unreviewed;       658 AA.
AC   A0A1I2YYF0;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:SFH30678.1};
GN   ORFNames=SAMN04489864_108184 {ECO:0000313|EMBL:SFH30678.1};
OS   Pedobacter insulae.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Pedobacter.
OX   NCBI_TaxID=414048 {ECO:0000313|EMBL:SFH30678.1, ECO:0000313|Proteomes:UP000199666};
RN   [1] {ECO:0000313|EMBL:SFH30678.1, ECO:0000313|Proteomes:UP000199666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 18684 {ECO:0000313|EMBL:SFH30678.1,
RC   ECO:0000313|Proteomes:UP000199666};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) 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; FOPP01000008; SFH30678.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I2YYF0; -.
DR   STRING; 414048.SAMN04489864_108184; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000199666; 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:UP000199666}.
FT   DOMAIN          341..514
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   658 AA;  73739 MW;  B6BE2DD9584E2016 CRC64;
     MQFDRKDKDD QFLLALYKRL LYPRMVEEKM LILLRQGRIG KWFSGIGQEA IAVGSTLAMQ
     CDEYILPMHR NLGVFTARDI PLKKLMAQWQ GKLSGFTKGR DRSFHFGTQD YKIIGMISHL
     GPQMALADGI ALADVIANKQ HATLVFTGEG ATSEGDFHEA INVASVWKLP VIFLIENNGY
     GLSTPINEQF NCKHLVDRAI GYGIEGHQID GNNVLEVYDK LDQIAKDIRT NPRPILVECL
     TFRMRGHEEA SGVKYVPQEL FEEWAGKDPV KTFEKYLIEQ NILTDDLIPS IKTEIKKAIE
     WDIEAAFDEE EPIANAMLEL VDMYYPYQQS VSRATEGQTE KRYLDAITDG LREGMKRFEN
     MIIMGQDIAE YGGAFKITDG FVNEFGKARV RNTPICESAI VGAALGLSIN GYKAVMEMQF
     ADFVTCGFNQ IVNNLAKTHY RWREKADVVI RMPTGAGTGA GPFHSQSNEA WFTKTPGLKV
     VYPAFPYDAK GLLIAAIEDP NPVMYFEHKY LYRSLTGLVP TGYYTVEIGK ANVLKKGTQI
     SIITYGLGVH WALDYLKEHP EVSATLVDLV SLQPWDKETV SAAVKASGRV LILHEDTLSS
     GFGAEVAAWI GEHCFSDLDA PVMRCASLDT AIPMNKVLED DFLAKKRLGE MVEKLLKY
//