ID A0A1H4DH49_9BURK Unreviewed; 672 AA.
AC A0A1H4DH49;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=SAMN05192564_102823 {ECO:0000313|EMBL:SEA71572.1};
OS Paraburkholderia sartisoli.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=83784 {ECO:0000313|EMBL:SEA71572.1, ECO:0000313|Proteomes:UP000198638};
RN [1] {ECO:0000313|EMBL:SEA71572.1, ECO:0000313|Proteomes:UP000198638}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 24000 {ECO:0000313|EMBL:SEA71572.1,
RC ECO:0000313|Proteomes:UP000198638};
RA de Groot N.N.;
RL Submitted (OCT-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 -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; FNRQ01000002; SEA71572.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H4DH49; -.
DR STRING; 83784.SAMN05192564_102823; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000198638; 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; 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:UP000198638};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 359..531
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 672 AA; 72704 MW; FA84F8151DD2C911 CRC64;
MTTSSPAPTS QMANAIRALA MDAVQKANSG HPGMPMGMAE IGVALWSRHL RHNPKNPQWF
DRDRFVLSNG HGSMLLYSLL HLTGYDLPME ELKNFRQLHS KTPGHPEYGI TPGVETTTGP
LGQGLANAVG MALAESLLAN EFNKPDAKIV DHRTYVFVGD GCLMEGISHE ACSLAGVLKL
NKLIAFYDDN GISIDGEVIH WFRDDTPKRF EAYGWNVIPG VIGHDVEAVD AAIKQAKQSD
RPTLICCKTV IGEGAPTKAG SHDAHGAPLG DKEIAATRAK IGWNYEPFVI PPEVYAAWDA
KESGAKIEGE WDKAFAAYRA KYPQEAADFE RRMSKQLPAD WAQKAQAIIA GANERAETVA
TRKASQQAIE GLSAVLPELL GGSADLTGSN LTNWKAAKYV RVGENGAAGN YVNYGVREFG
MSAAINGIAV HGGFKAFGGT FLTFSDYSRN ALRVAALMKA PSIFVFTHDS IGLGEDGPTH
QSIEHVSSLR MIPHMQVWRP ADTVETAVSW TQAVEHHGPS CLIFSRQNLA FSERTDAQIA
NIAKGGYVLR DWNDEIPARK IILIATGSEV ELALKAIEPL AQAGIGARVV SMPSTTVFDQ
QDAAYRERVL PQGVRRVAIE AGVTDFWRKY VGLEGGVVGI DVFGESAPAN VLFPFFGFTV
EHVVETAKKT LG
//
