ID Q5M4C5_STRT2 Unreviewed; 337 AA.
AC Q5M4C5;
DT 01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT 01-FEB-2005, sequence version 1.
DT 24-JAN-2024, entry version 89.
DE RecName: Full=Pyruvate dehydrogenase E1 component subunit beta {ECO:0000256|ARBA:ARBA00016138};
DE EC=1.2.4.1 {ECO:0000256|ARBA:ARBA00012281};
GN Name=acoB {ECO:0000313|EMBL:AAV60702.1};
GN OrderedLocusNames=stu1050 {ECO:0000313|EMBL:AAV60702.1};
OS Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=264199 {ECO:0000313|EMBL:AAV60702.1, ECO:0000313|Proteomes:UP000001170};
RN [1] {ECO:0000313|EMBL:AAV60702.1, ECO:0000313|Proteomes:UP000001170}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-250 / LMG 18311 {ECO:0000313|Proteomes:UP000001170};
RX PubMed=15543133; DOI=10.1038/nbt1034;
RA Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D., Fonstein M.,
RA Overbeek R., Kyprides N., Purnelle B., Prozzi D., Ngui K., Masuy D.,
RA Hancy F., Burteau S., Boutry M., Delcour J., Goffeau A., Hols P.;
RT "Complete sequence and comparative genome analysis of the dairy bacterium
RT Streptococcus thermophilus.";
RL Nat. Biotechnol. 22:1554-1558(2004).
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}.
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DR EMBL; CP000023; AAV60702.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5M4C5; -.
DR STRING; 264199.stu1050; -.
DR KEGG; stl:stu1050; -.
DR eggNOG; COG0022; Bacteria.
DR HOGENOM; CLU_012907_1_1_9; -.
DR OMA; PVMIFEH; -.
DR Proteomes; UP000001170; Chromosome.
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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001170}.
FT DOMAIN 12..187
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 337 AA; 36287 MW; BC78039D32695DCA CRC64;
MSNTSMSETK LMALREAVNL AMSEEMRKDP DIFLMGEDVG IYGGDFGTSV GMLAEFGEKR
VKDTPISEAA IAGAAVGAAI TGLRPIVDLT FMDFITIALD AIVNNGAKNN YMFGGGLKTP
VTFRVASGSG IGSAAQHSQS LESWLTHIPG IKVVAPGNAN DAKGLLKSSI QDNNIVIFME
PKALYGKKEE VTQDPDFYIP LGKGEIKREG TDLTIVTYGR MLERVLKAAE EVAEQGINVE
VVDPRTLVPL DKELIFESVK KTGKLMLVND AYKTGGFIGE IAAMVTESEA FDYLDHPIVR
LASEDVPVPY ARVLEQAVLP DVEKIKAAII KMANKGN
//