ID A0A063BFY2_9BURK Unreviewed; 673 AA.
AC A0A063BFY2;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=LIG30_0723 {ECO:0000313|EMBL:KDB10380.1};
OS Burkholderia sp. lig30.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB10380.1, ECO:0000313|Proteomes:UP000027020};
RN [1] {ECO:0000313|EMBL:KDB10380.1, ECO:0000313|Proteomes:UP000027020}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA Brown S.D., Hazen T.C.;
RT "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT Isolated from Wet Tropical Forest Soil.";
RL Submitted (MAR-2014) 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}.
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:KDB10380.1}.
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DR EMBL; JGVW01000022; KDB10380.1; -; Genomic_DNA.
DR RefSeq; WP_038709200.1; NZ_JGVW01000022.1.
DR AlphaFoldDB; A0A063BFY2; -.
DR STRING; 1192124.LIG30_0723; -.
DR PATRIC; fig|1192124.4.peg.357; -.
DR eggNOG; COG0021; Bacteria.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000027020; 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:UP000027020};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDB10380.1}.
FT DOMAIN 359..532
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 673 AA; 72611 MW; 4059871AC34AE1CA CRC64;
MTTSSPSTPT LMANAIRALA MDAVQQANSG HPGMPMGMAE IGVALWSRHL KHNPANPHWA
DRDRFVLSNG HGSMLLYALL HLTGYDLPIG ELKNFRQLHS KTPGHPEYGI TAGVETTTGP
LGQGLANAVG MALGEALMAA EFNRDDAKIV DHHTYVFLGD GCLMEGISHE ACSFAGTLKL
NKLIALYDDN GISIDGDVVN WFHDDTPKRF ESYGWNVIPD VNGHDVDAVD AAIAKAKLSD
KPTLICCKTR IGEGAATKAG GHDVHGSPLG AEEIAKTREA LGWKWEPFVI PQEVYAAWDA
KEAGTRRESD WNAVFGQYRA KYPQEAAEFE RRMAGKLPAD WAGKAAAIVA GANARGETVA
TRKASQQAIE GLAAVLPELL GGSADLTGSN LTNWKASKPV RAGENGIQWG NHINYGVREF
GMSAAINGLV LHGGYKPFGG TFLTFSDYSR NALRVAALMK VPSIFVFTHD SIGLGEDGPT
HQSIEHVASL RLIPGHDVWR PADTVETAVA WTYAVAHQGP SSLIFSRQNL QFNERTDTQI
ANIEKGGYVL RDWDEEIVAR KIILIATGSE VELAMKAVEP LARQGIAARV VSMPATTVFD
RQDAEYRERV LPHGVRRIAI EAGVTSFWHK YVGLEGGVVG IDTFGESAPA GVLFKHFGFT
VDKVVETAKA VLA
//
