ID   A0A1A9BR29_9ACTN        Unreviewed;       684 AA.
AC   A0A1A9BR29;
DT   05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2016, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=GA0115233_101427 {ECO:0000313|EMBL:SBT89984.1};
OS   Streptomyces sp. DI166.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1839783 {ECO:0000313|EMBL:SBT89984.1, ECO:0000313|Proteomes:UP000198690};
RN   [1] {ECO:0000313|Proteomes:UP000198690}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DI166 {ECO:0000313|Proteomes:UP000198690};
RA   Varghese N., Submissions Spin;
RL   Submitted (JUN-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; FLSP01000014; SBT89984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1A9BR29; -.
DR   STRING; 1839783.GA0115233_101427; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000198690; Unassembled WGS sequence.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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   Reference proteome {ECO:0000313|Proteomes:UP000198690};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          367..544
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   684 AA;  73575 MW;  00EF43752249D4DC CRC64;
     MSTPDLEWTE LDRRAVDTAR LLAADAVQRA GHGHPGTAMS LAPVAYTLFQ KVMRHDPADP
     RWPGRDRFVL SAGHSSLTLY TQLYLGGFGL ELDDLKSFRT WGSRTPGHPE YGHTPGVETT
     TGPLGQGVAN GVGMAMAARY ERGLFDPGTP VGESPFDHFV YVIAGDGCLQ EGIAAEASSL
     AGHQKLGNLV LLWDDNHISI EGDTRTAVSE DVPGRYEAYG WHVQRVEPQA DGDVDPAALY
     AAIRAAQAET ERPSFIALRT IIAWPAPNAR NTEAAHGSAL GEEEVAATKR VLGFDPERTF
     EVSDEVVAHT RALVERGRAA RALWEKSLAE WRADNPGRAA EFDRIGAGQL PEGWEAAVPV
     FEPGRSMATR VASGKVLQGL GAVIPELWGG SADLAGSNNT TIDKTSSFLP KGNPLPEADP
     YGRTIHFGIR EHAMAAEMNG IALHGNTRIY GGTFLVFSDY MRNAVRMSAL MRLPVTYVWT
     HDSIGLGEDG PTHQPVEHLA SLRAIPGLNI VRPADANETA VAWREILRRD APHGLALTRQ
     GVPTYERNEA AAKGGYVLVD ASNGSPEVLL IATGSEVQLA VAARERLEAD GVPTRVVSMP
     SVEWFEEQEQ AYRDSVLPPA VRARVAVEAG VGLTWHKYVG DAGRIISLDH FGASADGNLL
     LREYGFTPQS VVAAARDSLS AAAR
//