ID   A0A1X7LRF2_9BURK        Unreviewed;       691 AA.
AC   A0A1X7LRF2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=SAMN06265784_108108 {ECO:0000313|EMBL:SMG56250.1};
OS   Paraburkholderia susongensis.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=1515439 {ECO:0000313|EMBL:SMG56250.1, ECO:0000313|Proteomes:UP000193228};
RN   [1] {ECO:0000313|Proteomes:UP000193228}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29540 {ECO:0000313|Proteomes:UP000193228};
RA   Varghese N., Submissions S.;
RL   Submitted (APR-2017) 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   -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; FXAT01000008; SMG56250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7LRF2; -.
DR   STRING; 1515439.SAMN06265784_108108; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000193228; 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; IPR020826; Transketolase_BS.
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.
DR   PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE   3: Inferred from homology;
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          371..543
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          112..134
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   691 AA;  75513 MW;  3D5C9814771D68C6 CRC64;
     MQNDPALDQL CINTIRTLSM DAVQKANSGH PGTPMALAPV AYQLWQHHLR YDPDEPLWPN
     RDRFVLSVGH ASMLLYSLLH LANVKAVDHD GKPTGAPAVS LDDIEHFRQI DSKTPGHPEY
     RMTTGVETTT GPLGQGLGNS VGMAMAARWY ENRFNQPDAP LFDYRVYALC GDGDMMEGIS
     HEAASIAGHL KLSNLIWIYD SNRVTIEGHT DLAYSDDVES RFRGYHWHTL HVDDANDTAA
     LDAALVEAKG VTDRPTLIVV HSIIGWGAPH KQDTSAAHGE PLGVEEVALA KKAYGWPEDK
     FFYVPDGVHE RFAQGIGARG KAAREQWQTQ FEAYKKQYPE YAREFAQIEA HELPQGWDGD
     IPSFDADAKG IATRESSGKV LNAIAARVPW LLGGAADLSP STKTNLKFEG AGSFEADNYG
     GRNLHFGIRE HAMGAIVNGL ALSNLRPFGS TFLIFSDYMK PPIRLSAIME VPAIYVFTHD
     SIGVGEDGPT HQPIEQLASL RGVPGLTVLR PGDANEVAEA WRIALSHPHR PSCIVVSRQP
     LPTLDRNRYA AASGVRHGAY VLADAPDGQK PQVILMATGS ELSICVDVYE KLKGEGIAAR
     VVSMPSWDIF EREDSAYQES VLPAGVEARV AVEQAAALGW DRYAGRLGAL VVMHTFGASA
     PLADLKKKFG FTPEHVYEAA KQQIERVRAK G
//