ID   A0A2H9VQY7_9SPHI        Unreviewed;       678 AA.
AC   A0A2H9VQY7;
DT   28-FEB-2018, integrated into UniProtKB/TrEMBL.
DT   28-FEB-2018, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   SubName: Full=2-oxoisovalerate dehydrogenase E1 component {ECO:0000313|EMBL:PJJ83224.1};
GN   ORFNames=CLV57_0202 {ECO:0000313|EMBL:PJJ83224.1};
OS   Mucilaginibacter auburnensis.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales;
OC   Sphingobacteriaceae; Mucilaginibacter.
OX   NCBI_TaxID=1457233 {ECO:0000313|EMBL:PJJ83224.1, ECO:0000313|Proteomes:UP000242687};
RN   [1] {ECO:0000313|EMBL:PJJ83224.1, ECO:0000313|Proteomes:UP000242687}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 28175 {ECO:0000313|EMBL:PJJ83224.1,
RC   ECO:0000313|Proteomes:UP000242687};
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 (NOV-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:PJJ83224.1}.
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DR   EMBL; PGFJ01000001; PJJ83224.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2H9VQY7; -.
DR   Proteomes; UP000242687; 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:UP000242687}.
FT   DOMAIN          361..534
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   678 AA;  75658 MW;  81F2DEB4A3675F99 CRC64;
     MLRVNYGLIH IPIVPSTKAV MNFDRKNLDN NTLIGIYRKL LLPRVIEEKM LVLLRQGRVG
     KWFSGIGQEA IAVGATMAMQ AEEYILPMHR NLGVFTTRNV PFERLLAQWV GKPSGFTKGR
     DRSFHFGSQE HKILGMISHL GPQPTLANGI ALADQLNKNG RATLVFVGEG TTSEGDFHEA
     LNIASVWNLP VIFLVENNGY ALSTPTNEQF NCKRLVDRAN GYGMEGRRID GNNILEVYYA
     INEIANSIRK QPRPALVECM TFRVRGHEEA SGTKYVPQEL LSEWQDKDPL RLFEEYLIAE
     GLFRREWGPY LRDEITARLE PLIEKVFAES NVQPDISEEL NDVYRESDLP QVAAESKNKV
     IRYIDAISAG LKQSMQKYDN LILMGQDIAE YGGVFKVTEG FVTEFGKDHV RNTPLCESGV
     IGAAMGLALN GYKALVEMQF ADFASSGFTQ IVNHLAKTHY RWGQNVDVVI RMPAGAGSAA
     GPFHSQSNEA WFIKTPGLKV VYPAFPDDAK GLLMAAIADP NPVMYFEHKY LYRNLMGKVP
     DGETYVEIGK ARVVKEGSAA TILTYGYAVH WALTYMAAHP DQDIELIDLR SLQPWDKATV
     IESVNKTGRA LVLHEDTLTC GFGAEVAACI AEQCFKHLDA PVMRCASLDT PVPMDKGLED
     QFLAKSRLEE AIKALLEY
//