ID   A0A1Q3T4H4_9CHLR        Unreviewed;       329 AA.
AC   A0A1Q3T4H4;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   24-JAN-2024, entry version 12.
DE   SubName: Full=Alpha-ketoacid dehydrogenase subunit beta {ECO:0000313|EMBL:OJV97176.1};
GN   ORFNames=BGO39_19560 {ECO:0000313|EMBL:OJV97176.1};
OS   Chloroflexi bacterium 54-19.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1895928 {ECO:0000313|EMBL:OJV97176.1, ECO:0000313|Proteomes:UP000186384};
RN   [1] {ECO:0000313|EMBL:OJV97176.1, ECO:0000313|Proteomes:UP000186384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=54-19 {ECO:0000313|EMBL:OJV97176.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJV97176.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; MKTJ01000036; OJV97176.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Q3T4H4; -.
DR   STRING; 1895928.BGO39_19560; -.
DR   Proteomes; UP000186384; Unassembled WGS sequence.
DR   GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR   CDD; cd07036; TPP_PYR_E1-PDHc-beta_like; 1.
DR   Gene3D; 3.40.50.920; -; 1.
DR   Gene3D; 3.40.50.970; -; 1.
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; 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); 1.
DR   SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE   4: Predicted;
FT   DOMAIN          4..179
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   329 AA;  36200 MW;  C15CAF3B5671EFBB CRC64;
     MAVKTVLEAV REALFEEMRR DENVFVLGED VGQRGGVFRV TDGLQKEFGE MRVLDTPLAE
     SAIAGVAIGA AVRGMRPVAE FQFADFIHPA VEQIIDEAAR FRYRSNNTFS CPVVFRAPYG
     GGVQGGMYHS QSVEAMFAMW PGLKVVTPSF PYDYKGLLKA AIRDNDPVVF FEHKKTYTLP
     SVKQEVPAGD YIVPLGKANV VKEGTNLSVF AYGMMLHQSL QAARVLEQEG VSVEVVDLRT
     LRPLDKETIL NSVKKTGRAL IVHEANLFGG FGGEIAAIIA EEAFEWLDAP VRRLAGLDVP
     GMPFALPLEE EFMPNPTKIA QAMRNLAAY
//