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Database: UniProt
Entry: H0BS94_9BURK
LinkDB: H0BS94_9BURK
Original site: H0BS94_9BURK 
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
//
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