ID G5S0D6_SALET Unreviewed; 217 AA.
AC G5S0D6;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE SubName: Full=Transketolase {ECO:0000313|EMBL:EHC99882.1};
GN ORFNames=LTSEURB_4623 {ECO:0000313|EMBL:EHC99882.1};
OS Salmonella enterica subsp. enterica serovar Urbana str. R8-2977.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=913084 {ECO:0000313|EMBL:EHC99882.1, ECO:0000313|Proteomes:UP000004776};
RN [1] {ECO:0000313|EMBL:EHC99882.1, ECO:0000313|Proteomes:UP000004776}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R8-2977 {ECO:0000313|EMBL:EHC99882.1,
RC ECO:0000313|Proteomes:UP000004776};
RX PubMed=21859443; DOI=10.1186/1471-2164-12-425;
RA den Bakker H.C., Moreno Switt A.I., Govoni G., Cummings C.A., Ranieri M.L.,
RA Degoricija L., Hoelzer K., Rodriguez-Rivera L.D., Brown S., Bolchacova E.,
RA Furtado M.R., Wiedmann M.;
RT "Genome sequencing reveals diversification of virulence factor content and
RT possible host adaptation in distinct subpopulations of Salmonella
RT enterica.";
RL BMC Genomics 12:425-425(2011).
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EHC99882.1}.
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DR EMBL; AFCW01001756; EHC99882.1; -; Genomic_DNA.
DR AlphaFoldDB; G5S0D6; -.
DR Proteomes; UP000004776; Unassembled WGS sequence.
DR GO; GO:0003824; F:catalytic activity; IEA:InterPro.
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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 1..78
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|Pfam:PF02779"
FT DOMAIN 94..209
FT /note="Transketolase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF02780"
SQ SEQUENCE 217 AA; 23557 MW; FA4B4C26623526D1 CRC64;
MAALMKQRQV MVYTHDSIGL GEDGPTHQPV EQVASLRVTP NMSTWRPCDQ VESAVAWKYG
VERQDGPTAL ILSRQNLAQQ ERTEEQLANI ARGGYVLKDC AGQPQIIFIA TGSEVELAVA
AYEKLTAEGV KARVVSMPST DAFDKQDAAY RESVLPKAVS ARVAIEAGIA DYWFKYVGLN
GAIVGMTTFG ESAPAELLFE EFGFTVDNVI AKAKALL
//
