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Database: UniProt
Entry: Q8CZF1_STRMU
LinkDB: Q8CZF1_STRMU
Original site: Q8CZF1_STRMU 
ID   Q8CZF1_STRMU            Unreviewed;       343 AA.
AC   Q8CZF1;
DT   01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT   01-MAR-2003, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   SubName: Full=Pyruvate dehydrogenase E1 component beta subunit {ECO:0000313|EMBL:AAN59086.1};
DE            EC=1.2.4.1 {ECO:0000313|EMBL:AAN59086.1};
GN   Name=pdhB {ECO:0000313|EMBL:AAN59086.1};
GN   OrderedLocusNames=SMU_1422 {ECO:0000313|EMBL:AAN59086.1};
OS   Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=210007 {ECO:0000313|EMBL:AAN59086.1, ECO:0000313|Proteomes:UP000002512};
RN   [1] {ECO:0000313|EMBL:AAN59086.1, ECO:0000313|Proteomes:UP000002512}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700610 / UA159 {ECO:0000313|Proteomes:UP000002512};
RX   PubMed=12397186; DOI=10.1073/pnas.172501299;
RA   Ajdic D., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA   Primeaux C., Tian R., Kenton S., Jia H., Lin S., Qian Y., Li S., Zhu H.,
RA   Najar F., Lai H., White J., Roe B.A., Ferretti J.J.;
RT   "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT   pathogen.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
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DR   EMBL; AE014133; AAN59086.1; -; Genomic_DNA.
DR   RefSeq; NP_721780.1; NC_004350.2.
DR   RefSeq; WP_002263118.1; NC_004350.2.
DR   AlphaFoldDB; Q8CZF1; -.
DR   STRING; 210007.SMU_1422; -.
DR   KEGG; smu:SMU_1422; -.
DR   PATRIC; fig|210007.7.peg.1266; -.
DR   eggNOG; COG0022; Bacteria.
DR   HOGENOM; CLU_012907_1_0_9; -.
DR   OrthoDB; 9771835at2; -.
DR   PhylomeDB; Q8CZF1; -.
DR   Proteomes; UP000002512; 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:SF3; ACETOIN:2,6-DICHLOROPHENOLINDOPHENOL OXIDOREDUCTASE SUBUNIT BETA; 1.
DR   PANTHER; PTHR43257; PYRUVATE DEHYDROGENASE E1 COMPONENT BETA SUBUNIT; 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:AAN59086.1};
KW   Pyruvate {ECO:0000313|EMBL:AAN59086.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002512}.
FT   DOMAIN          5..194
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   343 AA;  37170 MW;  8E2F88492B6D5652 CRC64;
     MARELLFMKA INEALDMAMA KDDKIILLGE DIAGGVKVKH LEEQNEEAWG GVMGVTSGLM
     AKYSRDRVID TPLSEHGYMS ASVGMALTGL HPVPELMFND FIGFCFDALI GQGSKMRYMF
     GGKAKVPMTV RTMHGAGASA AAQHSGSYYG IFGSIPGIKV VVPATPYDAK GLLLSALEDD
     NIVIFSEDKT LYGFKGEVPE DYYTVPIGKA VVRREGNDLT IVTIGKMLYV AYEVADRLAK
     DGISVEVIDL RTVAPWDQET VLNSVKKTGR LIVIDESNPH NNTATDIASV VNDKAFDYLD
     GPIKCVCAPN VPVPFAINLE QLYIPNADRV IEAAAELIDD LKA
//
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