ID   S7VF26_9BACT            Unreviewed;       806 AA.
AC   S7VF26;
DT   16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT   16-OCT-2013, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN   ORFNames=ADICYQ_2221 {ECO:0000313|EMBL:EPR68835.1};
OS   Cyclobacterium qasimii M12-11B.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cyclobacteriaceae;
OC   Cyclobacterium.
OX   NCBI_TaxID=641524 {ECO:0000313|EMBL:EPR68835.1, ECO:0000313|Proteomes:UP000014974};
RN   [1] {ECO:0000313|EMBL:EPR68835.1, ECO:0000313|Proteomes:UP000014974}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M12-11B {ECO:0000313|EMBL:EPR68835.1,
RC   ECO:0000313|Proteomes:UP000014974};
RX   PubMed=23950138;
RA   Shivaji S., Ara S., Singh A., Kumar Pinnaka A.;
RT   "Draft Genome Sequence of Cyclobacterium qasimii Strain M12-11BT, Isolated
RT   from Arctic Marine Sediment.";
RL   Genome Announc. 1:e00642-13(2013).
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:EPR68835.1}.
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DR   EMBL; ATNM01000091; EPR68835.1; -; Genomic_DNA.
DR   RefSeq; WP_020888697.1; NZ_ATNM01000091.1.
DR   AlphaFoldDB; S7VF26; -.
DR   STRING; 641524.ADICYQ_2221; -.
DR   PATRIC; fig|641524.5.peg.2201; -.
DR   eggNOG; COG0022; Bacteria.
DR   eggNOG; COG1071; Bacteria.
DR   OrthoDB; 9769337at2; -.
DR   Proteomes; UP000014974; Unassembled WGS sequence.
DR   GO; GO:0003863; F:3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; IEA:UniProtKB-EC.
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,
KW   ECO:0000313|EMBL:EPR68835.1}.
FT   DOMAIN          472..646
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   806 AA;  90186 MW;  924101571CBD41D9 CRC64;
     MNTEYFPTLT KESVNTFGVQ NVLNDYKLVM ISRHASLTVR KEVFMGKAKF GIYGDGKELA
     QIAMARFFQL GDFRSGYYRD QTLLFAMEEL SLQEYFAQLY AHTDIKVEPA TGGRLMNGHF
     STRSLNEDGS WKNLMKIKNS TADVSPTAAQ MPKLLGIAYA SKLFKANPAL HHMTEFSNKG
     REVAWGTIGN ASTAEGMFFE TFNAGGVLQV PMVISVWDDD YGISVTNDLQ VTKASISAAL
     EGFKRDNEHK GYEIIVVKGW DYEGLVNAYS RANKVAREQH VPVLVHVIEM TQPQGHSTSG
     SHERYKSKDR LAWEAEYDCV VKFKEYILDN KIASEEKLDQ IDAEAKQLVK ESKDKAWRAF
     TASIKKELDE AVVLLSELAK NTQGNEALFR MADELKQTLN PVRMDVISTV RKALLLVRTE
     PVEIKARLQN WYKSQSKLNE DRYSSHQYSE SEFRVGAIAP VEVSYADEPA LLDGREILKA
     CFDAILTRDP RVFVIGEDVG LIGDVNQAFA GLQAKHGDLR VTDTGIREVT IIGQGIGAAL
     RGLRPITEIQ YLDYLIYALM TLSDDLACLH YRTKGGQKAP LIIRTRGHRL EGVWHSGSPI
     GMILSSLRGI LLCVPRNMTQ AAGMYNTLLE SDQPAIVIET LNGYRLKEKM PSNIGDFKVA
     LGKAEILQEG KDITVVTYGS MCRIVMEAAK RLFTIGIYVE VIDVQTLMPF DLEQVILNSI
     KKTNRVVFAD EDVPGGASAF MMQQVLEMQN AYYYLDSQPM TLSAKEHRPA YSSDGDYFSK
     PSADDVVEKI YGVMHEADPG KYPSIF
//