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).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//