ID   A0A246FN52_9BACT        Unreviewed;       807 AA.
AC   A0A246FN52;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   24-JAN-2024, entry version 15.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=CDA63_05420 {ECO:0000313|EMBL:OWP64168.1};
OS   Hymenobacter amundsenii.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Hymenobacter.
OX   NCBI_TaxID=2006685 {ECO:0000313|EMBL:OWP64168.1, ECO:0000313|Proteomes:UP000197277};
RN   [1] {ECO:0000313|EMBL:OWP64168.1, ECO:0000313|Proteomes:UP000197277}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CCM 8682 {ECO:0000313|EMBL:OWP64168.1,
RC   ECO:0000313|Proteomes:UP000197277};
RA   Sedlacek I., Kralova S., Pantucek R., Svec P., Holochova P., Stankova E.,
RA   Vrbovska V., Busse H.-J.;
RT   "Hymenobacter amundsenii sp. nov. isolated from regoliths in Antarctica.";
RL   Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall
CC       conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple
CC       copies of three enzymatic components: pyruvate dehydrogenase (E1),
CC       dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase
CC       (E3). {ECO:0000256|ARBA:ARBA00025211}.
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC       {ECO:0000256|ARBA:ARBA00011870}.
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:OWP64168.1}.
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DR   EMBL; NIRR01000005; OWP64168.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A246FN52; -.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000197277; 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   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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR   PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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}.
FT   DOMAIN          473..647
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   807 AA;  90032 MW;  216FDB74795FA098 CRC64;
     MLTADPAAAM PTRVASLSKA DLLHDYRLGW ESRHASLAGR KEVFMGKAKF GIFGDGKELP
     QLAMARAFKA GDWRAGYYRD QTFMLAIGEL TLQQYFAQLY AHPDVEAEPA TAGRAMNGHF
     GTRHLDEDGQ FKNLAESKNS SADISPTGGQ MPRLVGLAYA SKLFRQNPDL HQFSQFSVNG
     NEVAFGTIGN ASTSEGMFFE AINAAGVLQI PMLISVWDDH YGISVPAEYQ TTKQNISEIL
     KGFQREGEGQ EGFEIYRVKG WDYATLVDTY QRAAEICRTE HVPVLIHVQE VTQPQGHSTS
     GSHERYKSTD RLSWEQEHDC LRKMREWLLA EGHATDEELD AIVKEAQETV KQARTAAWND
     FFNPIKQERD ELVVLLNKLV AETGTENNLH ELVEPLEHNP TPIRADLVRT VRRALRQVRS
     LRSGARRELQ NWLEQALAEN ADRYNSYLFS QSEEAVGNIT EVAVDYAADA ASVDGREVLQ
     ACFTANFERD PRIFAIGEDV GRIGDVNQAF AGLQDKFGEL RVTDTGIREC TIIGQGVGAA
     MRGLKPITEI QYLDYLIYGL EPLTDDVACL QYRTKGGQKA PLIVRTRGHR LEGIWHSGSP
     IQMILGAIRG IHLCVPRNMT QAAGFYNTLL RSDEPAIVIE CLNGYRLKEK MPSNPGEFTL
     PLGQPETLLR GSDLTIVTYG SMCRIVLDAA AQLAEVGINV EVIDVQTLLP FDLDHVIADS
     LRRTNRVLFA DEDVPGGGTA YMLQQVIDEQ QAYRFLDSQP RCLAAQAHRP PYGSDGDYFS
     KPNVEDVFDA VYEIMQEVDP KRFPAIY
//