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Database: UniProt
Entry: Q5M4C5_STRT2
LinkDB: Q5M4C5_STRT2
Original site: Q5M4C5_STRT2 
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
//
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