ID   A0A136KNA6_9CHLR        Unreviewed;       797 AA.
AC   A0A136KNA6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:KXK10763.1};
GN   Name=pdhB_2 {ECO:0000313|EMBL:KXK10763.1};
GN   ORFNames=UZ14_CFX002003150 {ECO:0000313|EMBL:KXK10763.1};
OS   Chloroflexi bacterium OLB14.
OC   Bacteria; Chloroflexota; Tepidiformia.
OX   NCBI_TaxID=1617415 {ECO:0000313|EMBL:KXK10763.1, ECO:0000313|Proteomes:UP000070321};
RN   [1] {ECO:0000313|EMBL:KXK10763.1, ECO:0000313|Proteomes:UP000070321}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OLB14 {ECO:0000313|EMBL:KXK10763.1};
RA   Speth D.R., In T Zandt M., Guerrero Cruz S., Jetten M.S., Dutilh B.E.;
RT   "Genome based microbial ecology of anammox granules in a full-scale
RT   wastewater treatment system.";
RL   Submitted (NOV-2015) 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:KXK10763.1}.
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DR   EMBL; LMZR01000072; KXK10763.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A136KNA6; -.
DR   STRING; 1617415.UZ14_CFX002003150; -.
DR   PATRIC; fig|1617415.3.peg.3199; -.
DR   Proteomes; UP000070321; 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   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   Pyruvate {ECO:0000313|EMBL:KXK10763.1}.
FT   DOMAIN          463..637
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   797 AA;  89707 MW;  2E8836B581197F90 CRC64;
     MPKKKGSIAL PLEKEEILKD YRLAYQSRQA SLIGRREVLS GKAKFGIFGD GKEIPQLAIA
     HAFQKGDWRS GYYRDQTWMF MLNAMSIQEF FAQLYAHADT TYDPASMGRQ MNAHFATRHL
     YPNGTWKSQT QLYNTSADIS PTGGQMPRSV GLAYASVLYR NIKELQNEKD FSINGNEVTF
     VTIGNASAAE GLFWESVNAI GVLKAPAVIS IYDDGYGISV PNDYQMTKGN IGKLLKGFER
     ENDSGFNLYS VPAWDYPALL ETYQNATDAA RENHIPALVH VFDVTQPQGH STSGSHERYK
     SAERLKWEEE FDGLKKMREW MIKERFVTSG ELDSVEKADY ESVEGFRKAA WEAYLSPITE
     ERNQLMDMFD ELASSSNHAS ELQMLKERLS SLPSYTRRDV HIFAHEALRI LYDESHPTKQ
     ILSAWKFDYD KINAERYGSH LYSGTAMNVS EVKPIYSDNS PTMFGFEVIN AAFDLALERE
     PRLVAFGEDV GKLGDVNQGF KGMQEKYGEL RVTDTGIREA TILGQAIGLG MRGLRPIAEI
     QYLDYVLYAL QTMSDDLATL YWRTAGGQKS PVIVRTRGHR LEGIWHAGSP MSGLMNLTRG
     MYVLVPRDMT RAAGFYNTLL QADEPAIVVE VLNGYRVKER LPDNIGEITV PLGVPEIIRN
     GKDVTVVTYG ACCRIVMDAA NKLSKFNIDV EVIDVQSLMP FDVHHHILES LKKTNRILFV
     DEDVPGGITA YMMQEVIEKQ GGYFHLDSPA KTLSAKAHRP AYGSDGDYWS KPSAESVFDA
     VYEMMNEVDP ALYPKIF
//