ID   A0A158AWI6_9BURK        Unreviewed;       697 AA.
AC   A0A158AWI6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=AWB78_02039 {ECO:0000313|EMBL:SAK62069.1};
OS   Caballeronia calidae.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777139 {ECO:0000313|EMBL:SAK62069.1, ECO:0000313|Proteomes:UP000071859};
RN   [1] {ECO:0000313|EMBL:SAK62069.1, ECO:0000313|Proteomes:UP000071859}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 29321 {ECO:0000313|EMBL:SAK62069.1};
RA   Oliw E.H.;
RL   Submitted (JAN-2016) 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; FCOX02000007; SAK62069.1; -; Genomic_DNA.
DR   RefSeq; WP_062604397.1; NZ_FCOX02000007.1.
DR   AlphaFoldDB; A0A158AWI6; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000071859; 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          375..547
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
FT   REGION          116..138
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   697 AA;  76377 MW;  3E40E6058750E7D3 CRC64;
     MSQATPQAKD LDQLTIDTIR TLSMDAVQKA NSGHPGTPMA LAPVAFHLWQ NHLRYDPDAP
     LWPNRDRFVL SVGHASMLLY SLLHLAGVKE FDDDGKPTGN PAVSLDDIEH FRQLDSKTPG
     HPEYRMTTGV ETTTGPLGQG LGNSVGMAMA ARWKEARFNK GKDAIFDYRV YALCGDGDMM
     EGVSHEAASL AGHLQLSNLI WIYDSNRITI EGHTDLAYSD DVEARFHGYN WHTLHVDDAN
     DAAALENAIN KAKSHTDKPT LIVVKSIIGW GAPNKQDTAS AHGEALGEEE VKLAKKFYGW
     PEDKQFYVPD GVMQHFADGM GARGKKLHAE WKQRFDAYAK SNPELAKEAW QMLESKLPDN
     WDADIPTFEP DAKGIATRDS SGKVLNAIAP RVPWLLGGAA DLAPSTKTNL KFEGAGSFEH
     DSYGGRNLHF GIREHGMGAV ANGLALSGLR PYASTFLIFS DYMKPPIRLS AIMEVPVIYV
     FTHDSIGVGE DGPTHQPIEQ LASLRGVPGL CTLRPADANE VSEVWRVALS QPKEPSCIVL
     TRQPLPTFDR KKYGSADGVK HGAYVLADTE AGKKPEVLLL ATGSEVSLCV EAYEKLKAEG
     IAARVVSMPS WDIFEKQDQA YKESVLPPDV HARVCVEQAA TLGWDRYVGR LGSQIVMHTF
     GASAPLKALK TKFGFTPERV YDEAKKQIAR VKSNGKE
//