ID F0FWW5_9BURK Unreviewed; 690 AA.
AC F0FWW5;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=B1M_02195 {ECO:0000313|EMBL:EGD06281.1};
OS Burkholderia sp. TJI49.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=987057 {ECO:0000313|EMBL:EGD06281.1, ECO:0000313|Proteomes:UP000003049};
RN [1] {ECO:0000313|EMBL:EGD06281.1, ECO:0000313|Proteomes:UP000003049}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TJI49 {ECO:0000313|EMBL:EGD06281.1,
RC ECO:0000313|Proteomes:UP000003049};
RX PubMed=23653265; DOI=10.1007/s11274-013-1366-5;
RA Khan A., Asif H., Studholme D.J., Khan I.A., Azim M.K.;
RT "Genome characterization of a novel Burkholderia cepacia complex genomovar
RT isolated from dieback affected mango orchards.";
RL World J. Microbiol. Biotechnol. 29:2033-2044(2013).
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:EGD06281.1}.
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DR EMBL; AEXE01000095; EGD06281.1; -; Genomic_DNA.
DR AlphaFoldDB; F0FWW5; -.
DR PATRIC; fig|987057.7.peg.378; -.
DR BioCyc; BSP987057:G10O5-3757-MONOMER; -.
DR Proteomes; UP000003049; 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; IPR049557; Transketolase_CS.
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.
DR PROSITE; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EGD06281.1}.
FT DOMAIN 374..549
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 690 AA; 74243 MW; 22FE9A64A13DBE50 CRC64;
MPPCPRFLDS FSGLDMTTSS PASTTLMANA IRALAMDAVQ QANSGHPGMP MGMAEIGVAL
WSRHLKHNPT NPHWADRDRF VLSNGHGSML LYSLLHLTGY DLPIEELKNF RQLHSKTPGH
PEYGITPGVE TTTGPLGQGL ANAVGMALGE ALLADEFNRD GAKIVDHHTY VFLGDGCLME
GISHEACSLA GTLKLNKLIA LYDDNGISID GDVVNWFHDD TPKRFEAYGW NVIPNVNGHD
VDAVDAAIAK AKQSDKPTLI CCKTVIGKGA ATKAGGHDVH GAALGAEEIA KTREALGWKW
EPFVIPQEVY AAWDAKEAGK RAESEWDATF AQYRAKYPAE AAEFERRMAN KLPADWAEKA
AAIIAGANER AETVATRKAS QQAIEGLAAA LPELLGGSAD LTGSNLTNWK ASKAVRANPE
GAGVLLGNHI NYGVREFGMS AAINGLALHG GHKPFGGTFL TFSDYSRNAL RVAALMKVPS
IFVFTHDSIG LGEDGPTHQS IEHVSSLRLI PNHDVWRPAD TVETAVAWTH AVAADRPSSL
IFSRQNLAFN PRTDAQIANI EKGGYVLKDW DEEIVARKII LIATGSEVEL AMKAVEPLAQ
QGIAARVVSM PSTSVFDRQD AEYRERVLPH GVRRVAIEAG VTSFWHKYVG LEGGVVGIDT
FGESAPAGVL FKYFGFTVEH VVETAKAVLA
//
