ID H5WTR8_9BURK Unreviewed; 683 AA.
AC H5WTR8;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=BurJ1DRAFT_0243 {ECO:0000313|EMBL:EHR69141.1};
OS Burkholderiales bacterium JOSHI_001.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales.
OX NCBI_TaxID=864051 {ECO:0000313|EMBL:EHR69141.1, ECO:0000313|Proteomes:UP000004674};
RN [1] {ECO:0000313|EMBL:EHR69141.1, ECO:0000313|Proteomes:UP000004674}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JOSHI_001 {ECO:0000313|EMBL:EHR69141.1,
RC ECO:0000313|Proteomes:UP000004674};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Mikhailova N., Zeytun A., Lu M., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Smith J., Lewis G.,
RA Woyke T.;
RT "Noncontiguous Finished sequence of Burkholderiales bacterium JOSHI_001.";
RL Submitted (NOV-2011) 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; CM001438; EHR69141.1; -; Genomic_DNA.
DR AlphaFoldDB; H5WTR8; -.
DR STRING; 864051.BurJ1DRAFT_0243; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_4; -.
DR OrthoDB; 8732661at2; -.
DR BioCyc; BBAC864051:G1H30-239-MONOMER; -.
DR Proteomes; UP000004674; Chromosome.
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; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
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; PS00801; TRANSKETOLASE_1; 1.
PE 3: Inferred from homology;
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004674};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 359..534
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 683 AA; 72394 MW; 6874EF66ACCD8E2C CRC64;
MPTTEQDTPL MANAVRALAM DAVQQANSGH PGAPMGMAEM AVALWGRHLK HNPANPHWAD
RDRFVLSNGH ASMLIYALLH LSGYALPLAE LKNFRQLHSR TPGHPEVDVT PGVETTTGPL
GQGVTNAVGM ALAEKLLAAE FNREGHAVVD HRTYVFLGDG CLMEGISHEA CALAGAWKLN
KLVALYDDNG ISIDGQVAPW YVDDVRKRFE GYGWNVIGPI DGHNVDAVDA ALNVAKQSTV
RPTLVVCKTH IGQGSPNRAG TSKAHGEPLG ADEIKLTRDK LGWAHAPFVI PDEAYAAWDA
KSRGAGEQAC WDEGFANYAK AFPELAAEFT RRMKGELPAG FAQAAVDAAV AAHTKADTVA
SRKASQIALE AFTKALPELL GGSADLTGSN LTNTSSTTAL RFDADGKPNG GRHINYGVRE
FGMAAIMNGI ALHGGFIPYG GTFLTFSDYS RNAIRMAALM KRRVVHVFTH DSIGLGEDGP
THQSVEHAAS LRLIPGLDVW RPADTAETAV AWACALQNAS RPSALLLSRQ NLPYAPKATS
GAAPDASGLD AIAKGGYVLA EPAEVGLDKK AQAVIIATGS EVQLALHAQA DLAKGGIAVR
VVSVPSTNVF DRQSVAYKRS VLPDGVPRVA IEAGVTDGWW KYGCAAVLGL DRYGESAPAP
LLFKHFHLTA QDLADTVRAV LGR
//
