ID A0A0L6T5F3_9BURK Unreviewed; 663 AA.
AC A0A0L6T5F3;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=AD742_17625 {ECO:0000313|EMBL:KNZ31382.1};
OS Methylibium sp. NZG.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Methylibium.
OX NCBI_TaxID=1686064 {ECO:0000313|EMBL:KNZ31382.1, ECO:0000313|Proteomes:UP000053102};
RN [1] {ECO:0000313|Proteomes:UP000053102}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bi G.;
RT "Draft Genome Sequences of the MTBE Degrading Bacterium Methylibium sp.
RT NZG.";
RL Submitted (JUL-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 -!- 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:KNZ31382.1}.
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DR EMBL; LGRD01000031; KNZ31382.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L6T5F3; -.
DR STRING; 1686064.AD742_17625; -.
DR PATRIC; fig|1686064.3.peg.1508; -.
DR Proteomes; UP000053102; 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:UP000053102};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KNZ31382.1}.
FT DOMAIN 348..523
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 663 AA; 70220 MW; F359682D7B7AD0C4 CRC64;
MANAIRALAM DAVQQANSGH PGAPMGMAEI AVALWGRHLR HNPAHPQWAD RDRFVLSNGH
GSMLLYALLH LSGYDLAVSE LRNFRQLHSK TPGHPESGLT PGVETTTGPL GQGVSNAVGM
ALAEKLLAKE FNRDGHEVVG HHTYVFLGDG CLMEGISHEA CALAGAWRLS KLVALYDDNG
ISIDGQVGPW FADDTPKRFE SYGWNVIAGV DGHDVDAVDA AIARAKTATQ PTLICCKTTI
GKGSPNRAGT AKAHGEALGA DEIKLTRAAL GWPHEPFVIP EDAYTLWDAK AVGTASEADW
DARFALYRAA FPDLAAEFTR RMRGDLPANW AQTAVDAAVA AHTKAETVAS RKASQLALEA
FTQALPELLG GSADLTGSNL TNTSSTPALR MAANGSPNGG RHINYGVREF GMAAVMNGVA
LHGGFIPYGG TFLTFSDYSR NAIRMAALMK LRVVHVFTHD SIGLGEDGPT HQSVEHAASL
RLIPGLDVWR PCDTAETAVA WACAIESKSR PSALLLSRQN LPYAPKARLD EIAKGGYVLA
EPSEVGLSKK AQAVIIATGS EVALALHAQQ QLAILGIAVR VVSMPSTNVF DRQSAAYKAS
VLPANAPRIA VEMGVTDGWW KYGCAAVVGI DSYGESAPAP VLFKHFGFTA DNVAATVRAV
LGR
//
