ID   C5CS81_VARPS            Unreviewed;       701 AA.
AC   C5CS81;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   27-MAR-2024, entry version 76.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:ACS21861.1};
GN   OrderedLocusNames=Vapar_5259 {ECO:0000313|EMBL:ACS21861.1};
OS   Variovorax paradoxus (strain S110).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=543728 {ECO:0000313|EMBL:ACS21861.1};
RN   [1] {ECO:0000313|EMBL:ACS21861.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S110 {ECO:0000313|EMBL:ACS21861.1};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA   Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Ovchinnikova G., Orwin P.,
RA   Leadbetter J.R., Spain J.C., Han J.I.;
RT   "Complete sequence of chromosome 1 of Variovorax paradoxus S110.";
RL   Submitted (JUN-2009) 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   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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DR   EMBL; CP001635; ACS21861.1; -; Genomic_DNA.
DR   AlphaFoldDB; C5CS81; -.
DR   STRING; 543728.Vapar_5259; -.
DR   KEGG; vap:Vapar_5259; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_4; -.
DR   OrthoDB; 8732661at2; -.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016744; F:transketolase or transaldolase activity; IEA:UniProt.
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; IPR033248; Transketolase_C.
DR   InterPro; IPR049557; Transketolase_CS.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
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}.
FT   DOMAIN          355..560
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   701 AA;  75058 MW;  4CFB793A49A03793 CRC64;
     MANQALMANA IRALAMDAVQ QANSGHPGAP MGMADMAVAL WGEHLRYNPA NPHWFDRDRF
     VLSNGHASML LYSVLHLTGY DLPISELKNF RQLHSKTAGH PEVDVTPGVE TTTGPLGQGI
     TNAVGFALAE KLLAAEFNRK DHAIVDHHTY AFLGDGCMME GISHEACALA GAWHLNKLIA
     LYDDNGISID GQVKPWFIDN TEERFKAYGW NVIGPIDGND AKDVSKAIAK AKKEDSKPTL
     IICKTQIGKG SPNRANTAKA HGEPLGADEI ALTRAALNWP YAAFEVPQEA YADWNHKEEG
     AKAEAAWNDR FDAYAKAYPG LAAEFTRRMK GELPKNFHQV AFDTVVAAHT KGETVASRKA
     SQLALEAFTA ALPEMLGGSA DLTGSNLTNT KSTAALRFDA KTGAVVLNAP IATQSPQGAE
     DEAAQGAAVE PPHGEIGRHI NYGVREFGMA AIMNGIALHG GFIPYGGTFL TFSDYSRNAI
     RMAALMKRRV VHVFTHDSIG LGEDGPTHQS IEHAASLRLI PNLDVWRPGD TAETAVAWAV
     ALQNQSRPTA LLLSRQNIAY APKGDLGDIS RGAYVLSEPE AVGLKSKKTA AVIIATGSEV
     QLALAAQKLL AEKKIAVRVV SMPSTTTFDR QDVAYKKAVL PKKLPRIAVE MGCTGGWWKY
     GCAAVVGIDS YGESAPAPAL FKHFGFTAEN VAATVEAALR G
//