ID A0A0Q7AEL3_9BURK Unreviewed; 687 AA.
AC A0A0Q7AEL3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=ASC76_12945 {ECO:0000313|EMBL:KQW38866.1};
OS Rhizobacter sp. Root404.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Rhizobacter.
OX NCBI_TaxID=1736528 {ECO:0000313|EMBL:KQW38866.1, ECO:0000313|Proteomes:UP000051611};
RN [1] {ECO:0000313|EMBL:KQW38866.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW38866.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW38866.1, ECO:0000313|Proteomes:UP000051611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root404 {ECO:0000313|EMBL:KQW38866.1,
RC ECO:0000313|Proteomes:UP000051611};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQW38866.1}.
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DR EMBL; LMDS01000004; KQW38866.1; -; Genomic_DNA.
DR RefSeq; WP_056466245.1; NZ_LMDS01000004.1.
DR AlphaFoldDB; A0A0Q7AEL3; -.
DR STRING; 1736528.ASC76_12945; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000051611; 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:UP000051611};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQW38866.1}.
FT DOMAIN 368..543
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 687 AA; 73209 MW; DA4E0410D42F37E8 CRC64;
MATHSNTTNA TLMANSIRAL AMDAVQQANS GHPGAPMGMA DMAVALWGRH LRHNPGNPQW
ANRDRFVLSN GHASMILYAL LHLTGYDLPM SELRNFRQLH SKTPGHPEHG LTPGVETTTG
PLGQGIANAV GMALAEKLLA KEFNRDGHAI VDHHTYVFLG DGCMMEGISH EAAALAAAWK
LGKLIALYDD NGISIDGQVK PWFVDNTPER FRAYGWNVIA DVDGHDADAI DAAIRQAIAQ
GGGTGPGGGR PTLICCKTVI GQGSPNRAGT AKAHGEALGA DEIKLTREAI GWTSEPFVIP
EESYSLWDAR QQGLADETAW VDAFAAYAKA YPELAVEFAR RMDNELPKNW SQTVVDAAVA
AQTKAETVAS RKASQLALEA FTKALPELIG GSADLTGSNL TNTSSTAPFR LEADGSSNGG
RHINYGVREF GMAAVMNGIA LHGGLIPYGG TFLTFSDYSR NAIRMAALMK QRVIHVFTHD
SIGLGEDGPT HQSIEHAASL RLIPGLDVWR PCDTAETVIA WACAIENTGR PSALLLSRQN
LPYAPKKSLD GISKGGYVLA EPSEVGLNKK AQAVIIATGS EVQLALHAQQ ELAKRENGGI
AVTVVSMPST TVFDRQTEAY KTSVLPKGVP RIAVEMGVTG GWWKYGCAAV VGIDTYGESA
PAPVLFKHFG FTTENVVATV RQALGKR
//
