ID A0A2X3GKT2_9LIST Unreviewed; 222 AA.
AC A0A2X3GKT2;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 27-MAR-2024, entry version 15.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:SQC68862.1};
DE EC=2.2.1.1 {ECO:0000313|EMBL:SQC68862.1};
GN Name=tkt_4 {ECO:0000313|EMBL:SQC68862.1};
GN ORFNames=NCTC13940_01290 {ECO:0000313|EMBL:SQC68862.1};
OS Listeria fleischmannii subsp. fleischmannii.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1671902 {ECO:0000313|EMBL:SQC68862.1, ECO:0000313|Proteomes:UP000250257};
RN [1] {ECO:0000313|EMBL:SQC68862.1, ECO:0000313|Proteomes:UP000250257}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13940 {ECO:0000313|EMBL:SQC68862.1,
RC ECO:0000313|Proteomes:UP000250257};
RG Pathogen Informatics;
RA Doyle S.;
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
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; UAWT01000012; SQC68862.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2X3GKT2; -.
DR Proteomes; UP000250257; Unassembled WGS sequence.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR Pfam; PF02779; Transket_pyr; 1.
DR Pfam; PF02780; Transketolase_C; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 1.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000250257};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SQC68862.1}.
FT DOMAIN 1..74
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|Pfam:PF02779"
FT DOMAIN 99..207
FT /note="Transketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02780"
SQ SEQUENCE 222 AA; 24007 MW; 88E65D3E2D3BE2FE CRC64;
MKLPVTYVFT HDSIAVGEDG PTHEPIEHLA SLRAMPGLSV LRPADAKETR VAWEEAMQNQ
DGPVALVLSR QDLPVLETAQ ETVTSGVKKG AYIVSPSEKE MPDAILIATG SEVSLAIAAQ
NELKSRHIDV SVVSLPSFDI FKQQSKAYQE SVLPNAVRAR FAIEAASTFG WHDIIGDAGE
MLGIDHFGAS APAERLFEAF GFTKENVADR VQKLVEKAGV RV
//