ID H0BS94_9BURK Unreviewed; 688 AA.
AC H0BS94;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=KYG_01152 {ECO:0000313|EMBL:EHL24736.1};
OS Acidovorax sp. NO-1.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=512030 {ECO:0000313|EMBL:EHL24736.1, ECO:0000313|Proteomes:UP000003485};
RN [1] {ECO:0000313|EMBL:EHL24736.1, ECO:0000313|Proteomes:UP000003485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NO-1 {ECO:0000313|EMBL:EHL24736.1,
RC ECO:0000313|Proteomes:UP000003485};
RX PubMed=22374962; DOI=10.1128/JB.06814-11;
RA Huang Y., Li H., Rensing C., Zhao K., Johnstone L., Wang G.;
RT "Genome Sequence of the Facultative Anaerobic Arsenite-Oxidizing and
RT Nitrate-Reducing Bacterium Acidovorax sp. Strain NO1.";
RL J. Bacteriol. 194:1635-1636(2012).
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; AGTS01000012; EHL24736.1; -; Genomic_DNA.
DR RefSeq; WP_008902962.1; NZ_AGTS01000012.1.
DR AlphaFoldDB; H0BS94; -.
DR STRING; 512030.KYG_01152; -.
DR PATRIC; fig|512030.4.peg.221; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000003485; 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; 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:UP000003485};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..35
FT /note="Transketolase signature 1"
FT /evidence="ECO:0000259|PROSITE:PS00801"
SQ SEQUENCE 688 AA; 73690 MW; 1956C3280F8C059B CRC64;
MANTQQSQQM ANAIRALAMD AVQQANSGHP GAPMGMADMA VGLWARHLKH NPTNPQWFDR
DRFVLSNGHG SMLLYALLHL SGYNLPIGEL KNFRQLHSKT AGHPEVGVTP GVETTTGPLG
QGITNAVGFA LAEKLLAAEF NREGHAVVDH NTFVFLGDGC LMEGISQEAI SLAGAWKLNK
LVALYDDNGI SIDGQVLPWF ADNTALRFVS AGWNVIGPID GHDADKVADA VAEAKKQSER
PSLIICKTHI GKGSPNRVNT AKAHGEPLGA EEIALTREAL GWSSEPFVIP EDVYASWDAK
SNGQKAEAAW NDRFAAYSKA FPELAAELTR RMNGDLPANF AQVAVDTVVA AHTKGETVAS
RKASQLALEA FTAALPELLG GSADLTGSNL TNTKSTPNLR FDMQGAVVKT EAANGDKVGG
RHINYGVREF GMAAIMNGVA LHGGFIPYGG TFLTFSDYSR NAIRMAALMK QRVIHVFTHD
SIGLGEDGPT HQSIEHVASL RLIPNLDVWR PADTAETAVA WSVALSNRNK PTVLALSRQN
LQHLSALAPK RNLGDISRGA YVLSEPADVG IKKKPVAVII ATGSEVQLAL KAQRLLADKK
VPVRVVSMPS TTTFDREDAK YKSSVLPAGV PRVAVEMGVT DSWWKYGCAA VVGIDTYGES
APAPVLFKHF GFTEENVAAT VLAVLRRR
//