ID   A0A0F0HTN4_9PSEU        Unreviewed;       701 AA.
AC   A0A0F0HTN4;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=UK12_18985 {ECO:0000313|EMBL:KJK57058.1};
OS   Saccharothrix sp. ST-888.
OC   Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharothrix.
OX   NCBI_TaxID=1427391 {ECO:0000313|EMBL:KJK57058.1, ECO:0000313|Proteomes:UP000033409};
RN   [1] {ECO:0000313|EMBL:KJK57058.1, ECO:0000313|Proteomes:UP000033409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ST-888 {ECO:0000313|EMBL:KJK57058.1,
RC   ECO:0000313|Proteomes:UP000033409};
RA   Ju K.-S., Doroghazi J.R., Metcalf W.;
RL   Submitted (FEB-2015) 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}.
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:KJK57058.1}.
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DR   EMBL; JYJF01000057; KJK57058.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0F0HTN4; -.
DR   PATRIC; fig|1427391.3.peg.5712; -.
DR   Proteomes; UP000033409; 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:UP000033409};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          371..551
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   701 AA;  75062 MW;  5F5FB0727DACBE13 CRC64;
     MPSSATDFEW TELDRRTVDV ARALAADAVE AAGHGHPGTA MSLAPAAYLL FQRLLRHDPS
     DPAWAGRDRF VLSCGHSSLT LYIQLFLSGY GLTLDDLKAL RTAGSLTPAH PEYGHTPGVE
     TTTGPLGQGF ANAVGMAMAA RRERGLFDPS AAPEQSPFDH TIWVFASDGD LEEGISHEAS
     AIAGHQKLGN LVVLYDDNHI SIEDDTQIAV SEDVLARYAA YGWHVQRVDW TGTGEYVEDV
     AQLHGALDAA RAETGRPSIV ALRTIIGWPA PTKQNTGKIH GSALGAAEVA ATKQALGLDP
     AKSFDVPAEL LDHARQVVER GRQARQEWEK SFGDWRAAEP ARAAEFDRIS TRTLPAGWSS
     ALPEFPAGTE VATRKASGEV LSALAPVLPE LWGGSADLAE SNLTTMKGEP SFVPEELQTA
     AFKGHRYGRT LHFGIREHGM GGILNGIALH GGTRPYGGTF LVFSDYMRPS VRLAAMMNLP
     VTYVWTHDSI GLGEDGPTHQ PVEHLASLRA IPGLDVVRPA DANETVVAWR TIIENTDRPA
     GLCLSRQNLP VLERTSATGL AAAEGAARGG YVLAEAAGDA PEVILIATGS EVPIALRARE
     ILQAEGTATR VVSMPCVEWF DEQDAAYRES VLPRGVRARV SVEAGSSLGW YALVGEAGES
     VGLDRFGLSA PYQTLYEQFG FTPERVAAHA RSSLAKARDR D
//