ID Q08ZP9_STIAD Unreviewed; 681 AA.
AC Q08ZP9;
DT 31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2006, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tkt {ECO:0000313|EMBL:EAU65931.1};
GN ORFNames=STIAU_1770 {ECO:0000313|EMBL:EAU65931.1};
OS Stigmatella aurantiaca (strain DW4/3-1).
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=378806 {ECO:0000313|EMBL:EAU65931.1, ECO:0000313|Proteomes:UP000032702};
RN [1] {ECO:0000313|EMBL:EAU65931.1, ECO:0000313|Proteomes:UP000032702}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DW4/3-1 {ECO:0000313|EMBL:EAU65931.1,
RC ECO:0000313|Proteomes:UP000032702};
RA Nierman W.C.;
RL Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate =
CC aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate;
CC Xref=Rhea:RHEA:10508, ChEBI:CHEBI:57483, ChEBI:CHEBI:57737,
CC ChEBI:CHEBI:58273, ChEBI:CHEBI:59776; EC=2.2.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00001027};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|ARBA:ARBA00001964};
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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:EAU65931.1}.
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DR EMBL; AAMD01000068; EAU65931.1; -; Genomic_DNA.
DR AlphaFoldDB; Q08ZP9; -.
DR PATRIC; fig|378806.16.peg.5016; -.
DR Proteomes; UP000032702; Unassembled WGS sequence.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR CDD; cd07033; TPP_PYR_DXS_TK_like; 1.
DR CDD; cd02012; TPP_TK; 1.
DR Gene3D; 3.40.50.920; -; 1.
DR Gene3D; 3.40.50.970; -; 2.
DR InterPro; IPR029061; THDP-binding.
DR InterPro; IPR009014; Transketo_C/PFOR_II.
DR InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR InterPro; IPR005478; Transketolase_bac-like.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR033247; Transketolase_fam.
DR InterPro; IPR005474; Transketolase_N.
DR NCBIfam; TIGR00232; tktlase_bact; 1.
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 Pfam; PF00456; Transketolase_N; 1.
DR SMART; SM00861; Transket_pyr; 1.
DR SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
DR SUPFAM; SSF52922; TK C-terminal domain-like; 1.
PE 3: Inferred from homology;
KW Transferase {ECO:0000313|EMBL:EAU65931.1}.
FT DOMAIN 380..550
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 681 AA; 75286 MW; 81A44B6D087EC3C8 CRC64;
MRPRKPRTFL MTTDSQDLKC INTLRTLAMD AVEKAHSGHP GAPMALAPVA YQLWQQELRY
DPTNPLWPNR DRFVLSNGHA SMLLYGLLHL SGVRRVSKEL RVEDAPAVSL EDIQKFRQLD
SATPGHPEYR WTSGVETTTG PLGQGVANSV GMAMASRWLA GYFNRPDYTL FDYDVWTLCG
DGDLMEGVSS EAASLAGHLQ LPNLCWIYDS NHISIDGSTE LAFTEDVGRR FEAYGWRVLR
VEDANDLEAL SKAYRTFKEQ RGKPTLIIVH SRIGYGAPKK EGTASAHGEA LGAEEIKGAK
RKYGWPEDAQ FLVPEGVRER FQERLGTRGQ QTRAAWEQTL AGYKKAYPEL AEHLERMQRS
ELPEGWDKEL PVFPADAKGM ATRESGGKVL NALAKNYPWL VGGSADLNPS TKTYLTFSGP
MKPGDHTGRN VHFGVREHAM GSIVNGLTLS NLRGYGATFL IFSDYERPAI RLSSIMEIPS
IHIFTHDSIG LGEDGPTHQP VEQLLTLRSI PGLIVLRPAD ANEVTEAWRV IARQTHHPVA
LVLSRQPVPT LDRTKYAPAS GLSKGAYVLA DSEGTPDVIL IGTGTEVSLC LQAAEQLQSE
GVKARVVSMP SWELFEQQDE SYKDAVLLPS VRARVSVEQA AAFGWERWVG LTGKIIGMRT
FGASAPIKSL LQKSASPWRT W
//
