ID A0A3S9PFD3_STRLT Unreviewed; 693 AA.
AC A0A3S9PFD3;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN ORFNames=EKH77_07435 {ECO:0000313|EMBL:AZQ71059.1};
OS Streptomyces luteoverticillatus (Streptoverticillium luteoverticillatus).
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66425 {ECO:0000313|EMBL:AZQ71059.1, ECO:0000313|Proteomes:UP000267900};
RN [1] {ECO:0000313|EMBL:AZQ71059.1, ECO:0000313|Proteomes:UP000267900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 15060 {ECO:0000313|EMBL:AZQ71059.1,
RC ECO:0000313|Proteomes:UP000267900};
RA Feng Z., Chen G., Zhang J., Zhu H., Yu X., Zhang W., Zhang X.;
RT "The whole draft genome of Streptomyce luteoverticillatus CGMCC 15060.";
RL Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the transfer of a two-carbon ketol group from a
CC ketose donor to an aldose acceptor, via a covalent intermediate with
CC the cofactor thiamine pyrophosphate. {ECO:0000256|RuleBase:RU004996}.
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 ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 Mg(2+) ion per subunit. Can also utilize other divalent
CC metal cations, such as Ca(2+), Mn(2+) and Co(2+).
CC {ECO:0000256|RuleBase:RU004996};
CC -!- COFACTOR:
CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC Evidence={ECO:0000256|RuleBase:RU004996};
CC Note=Binds 1 thiamine pyrophosphate per subunit.
CC {ECO:0000256|RuleBase:RU004996};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738,
CC ECO:0000256|RuleBase:RU004996}.
CC -!- SIMILARITY: Belongs to the transketolase family.
CC {ECO:0000256|ARBA:ARBA00007131, ECO:0000256|RuleBase:RU004996}.
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DR EMBL; CP034587; AZQ71059.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S9PFD3; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000267900; Chromosome.
DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProt.
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; 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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|RuleBase:RU004996};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Reference proteome {ECO:0000313|Proteomes:UP000267900};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 371..552
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 693 AA; 74925 MW; E835090877AF4226 CRC64;
MSTKPTTTDL EWTELDQRAV DTARVLAMDS VQKVGNGHPG TAMSLAPAAY LLFQKLMRHD
PSDAGWVGRD RFVLSPGHTS LTLYTQLFLS GYGLELGDLK AFRTWDSKTP GHPEHGHTVG
VETTTGPLGQ GIANAVGMAM AARYERGLFD PEAPKGESPF DHTVWAIVSD GDLEEGISAE
ASSLAGHQKL GNLVALYDDN HISIEGDTET AFSEDVLKRY EAYGWHVQRI EQGANGDFDI
KALYAAFQAA KAETERPSII AARTIIAWPA PNAQNTEASH GSALGEAEVA ATKKVMGFDP
EQHFQVEDEV LAHARQVVDR GRAARAAWDK QVQVWREANP ERAADFDRIV AGELPDGWEK
ALPVFPAGKD VATRKASGEV LKALGGVIPE LWGGSADLAG SNNTTIDATS SFLPEGNPLP
EANPYGRTIH FGIREHAMGS TMNGIALHGN TRVYGGTFLV FSDYMRPAVR LAALMKLPVT
YVWTHDSIGL GEDGPTHQPV EHMAALRAIP GLNMVRPADA NETAIAWREI VKRHTTKPAP
HGLALTRQNV PTYEANEGTA KGGYVLFDAE GGRPQVILIA TGSEVQLAVE AREALQADGV
PTRVVSMPSV EWFEEQDQAY RDGVLLPDVK ARVAVEAGIG LTWYRYVGEA GRIVSLEHFG
ASADYKVLYR EFGLTSDAVV EAARESIADA ARR
//
