ID A0A1X6YJ30_9RHOB Unreviewed; 671 AA.
AC A0A1X6YJ30;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN Name=tktA {ECO:0000313|EMBL:SLN22309.1};
GN ORFNames=ROH8110_00852 {ECO:0000313|EMBL:SLN22309.1};
OS Roseovarius halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=505353 {ECO:0000313|EMBL:SLN22309.1, ECO:0000313|Proteomes:UP000193207};
RN [1] {ECO:0000313|EMBL:SLN22309.1, ECO:0000313|Proteomes:UP000193207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8110 {ECO:0000313|EMBL:SLN22309.1,
RC ECO:0000313|Proteomes:UP000193207};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131}.
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DR EMBL; FWFU01000001; SLN22309.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YJ30; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000193207; 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; IPR020826; Transketolase_BS.
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; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000193207};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SLN22309.1}.
FT DOMAIN 357..528
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 671 AA; 72593 MW; 020EB179AE8F78F4 CRC64;
MDIAALRAAN PDHWTKAAAI RALTLDAVHA ANSGHSGMPM GMADVATVLF EKHLKFDAAA
PEWPDRDRFI LSAGHGSMLL YSLLYLTGNP DITLEEIRNF RQWGAKTAGH PENFLASGIE
TTTGPLGQGI SNAVGFAMAE EMLRARFGRK LVDHYTYVIA GDGCLMEGVS HEAIGIAGRQ
ALGKLIVFWD HNSITIDGKV DLSDRTDQVK RFRASGWQVL EIDGHDPAAI DAAITTARKS
RKPSMIACKT HIALGHAAQD TSKGHGALTD PDQLVAAKQA YGWPHGPFEV PGDVKSAWET
IGARGAAERE SWNARLGETS ERRQKEFARI FAGEAPKSLS ARIKALKKQV SEEKPKVATR
KSSEMVLEVV NPIMPETVGG SADLSGSNNT RSGDMSVFDV DNRKGRYVHW GIREHGMAAA
MNGMALHGGI RPYGGTFMCF TDYARPAMRL AALMKVPSVF VMTHDSIGLG EDGPTHQPVE
HLAISRATPN TWVFRPCDTV ETAEAWELAL RSTDTPSVLS LTRQGVPTLR HEHKNKNLTE
QGAYVLADAT GKRQAILIAT GSEVSVAMKA REMLEAEGIG TRVVSMPCME LFAAQDDAYR
KRVLPGGPVR VGVEAAIRQG WDRWLLGQGG REQKAGFVGM DSFGASAPAE TLFEKFGITA
EAVAQKVKSL L
//
