ID B9L123_THERP Unreviewed; 334 AA.
AC B9L123;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
GN OrderedLocusNames=trd_1734 {ECO:0000313|EMBL:ACM05123.1};
OS Thermomicrobium roseum (strain ATCC 27502 / DSM 5159 / P-2).
OC Bacteria; Thermomicrobiota; Thermomicrobia; Thermomicrobiales;
OC Thermomicrobiaceae; Thermomicrobium.
OX NCBI_TaxID=309801 {ECO:0000313|EMBL:ACM05123.1, ECO:0000313|Proteomes:UP000000447};
RN [1] {ECO:0000313|EMBL:ACM05123.1, ECO:0000313|Proteomes:UP000000447}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27502 / DSM 5159 / P-2
RC {ECO:0000313|Proteomes:UP000000447};
RX PubMed=19148287; DOI=10.1371/journal.pone.0004207;
RA Wu D., Raymond J., Wu M., Chatterji S., Ren Q., Graham J.E., Bryant D.A.,
RA Robb F., Colman A., Tallon L.J., Badger J.H., Madupu R., Ward N.L.,
RA Eisen J.A.;
RT "Complete genome sequence of the aerobic CO-oxidizing thermophile
RT Thermomicrobium roseum.";
RL PLoS ONE 4:E4207-E4207(2009).
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 -!- SUBUNIT: Heterodimer of an alpha and a beta chain.
CC {ECO:0000256|ARBA:ARBA00011870}.
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DR EMBL; CP001275; ACM05123.1; -; Genomic_DNA.
DR RefSeq; WP_015922676.1; NC_011959.1.
DR AlphaFoldDB; B9L123; -.
DR STRING; 309801.trd_1734; -.
DR KEGG; tro:trd_1734; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_0; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000000447; Chromosome.
DR GO; GO:0004739; F:pyruvate dehydrogenase (acetyl-transferring) activity; IEA:UniProtKB-EC.
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; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 1.
DR PANTHER; PTHR43257:SF2; PYRUVATE DEHYDROGENASE E1 COMPONENT SUBUNIT BETA; 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;
KW Oxidoreductase {ECO:0000313|EMBL:ACM05123.1};
KW Pyruvate {ECO:0000313|EMBL:ACM05123.1}.
FT DOMAIN 5..179
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 334 AA; 37211 MW; 28674AA11168FFC1 CRC64;
MAREITYRDA LREALREEMY RDERVFLMGE DIGAYGGSYA VTRGFLQEFG PDRVRDTPIA
ELGIVGLGIG AAIGGLRPVV ELMTVNFALL ALDQIVNHLA KIYYMFNGQF TAPVVVRTAE
GFGQLGATHS QFFENYFAYV PGLRVVAPAV PKDAKGFLKA AIRGNDPVIF IEHSLIYRNR
GEVPDGEDFL LPLEGAEVRR EGRDVTIVSW LRGYYLALGA AEELAREGIE CEVIDLRVLR
PLDVETIVRS VQKTNRLVIV EEGWKSFGVG AEIAASVQER ALDYLDAPIM RVASVEVPMP
YARNLERLVI PNKDKVIEAV REVLYQRLPA PVAR
//
