ID F0LJD0_THEBM Unreviewed; 308 AA.
AC F0LJD0;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:ADT83396.1};
GN OrderedLocusNames=TERMP_00419 {ECO:0000313|EMBL:ADT83396.1};
OS Thermococcus barophilus (strain DSM 11836 / MP).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=391623 {ECO:0000313|EMBL:ADT83396.1, ECO:0000313|Proteomes:UP000007478};
RN [1] {ECO:0000313|EMBL:ADT83396.1, ECO:0000313|Proteomes:UP000007478}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11836 / MP {ECO:0000313|Proteomes:UP000007478};
RX PubMed=21217005; DOI=10.1128/JB.01490-10;
RA Vannier P., Marteinsson V.T., Fridjonsson O.H., Oger P., Jebbar M.;
RT "Complete genome sequence of the hyperthermophilic, piezophilic,
RT heterotrophic, and carboxydotrophic archaeon Thermococcus barophilus MP.";
RL J. Bacteriol. 193:1481-1482(2011).
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DR EMBL; CP002372; ADT83396.1; -; Genomic_DNA.
DR AlphaFoldDB; F0LJD0; -.
DR KEGG; tba:TERMP_00419; -.
DR PATRIC; fig|391623.17.peg.419; -.
DR eggNOG; arCOG01051; Archaea.
DR HOGENOM; CLU_009227_1_1_2; -.
DR Proteomes; UP000007478; Chromosome.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
DR GO; GO:0006082; P:organic acid metabolic process; IEA:UniProt.
DR GO; GO:1901576; P:organic substance biosynthetic process; IEA:UniProt.
DR GO; GO:0044272; P:sulfur compound biosynthetic process; IEA:UniProt.
DR CDD; cd07033; TPP_PYR_DXS_TK_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; PTHR43825; PYRUVATE DEHYDROGENASE E1 COMPONENT; 1.
DR PANTHER; PTHR43825:SF1; TRANSKETOLASE-LIKE PYRIMIDINE-BINDING DOMAIN-CONTAINING PROTEIN; 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:UP000007478}.
FT DOMAIN 6..171
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 308 AA; 33912 MW; 3614B9CAC5032EC2 CRC64;
MDKIIESFRE AFGRALVEMG KENENVVVLD ADVKGSTKTI YFEKAFPGRF FQIGISEQDL
ISTAAGFAIA GKIPIASAFA AFMMRAWEQI RNTVARDNLN VKIVTTHSGF SDFMDGSSHQ
CLEDIALMRV LPNMRVLVPA DAYATRVLLE QMVESEGPFY MRLGRDYTVK VYDGEELKVG
KAEILREGED VFLIACGFMV SVALEVAEKL KDLSVGVADF HTIKPLDENT LLKIAKKVSL
IVTLEEHSIF GGLGGAVAEV LSEKIPKRVI RIGAEEFGRS SRDYLALLDF YGLSADKIAK
RIVKAVGG
//