ID B9DP72_STACT Unreviewed; 662 AA.
AC B9DP72;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 95.
DE RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662, ECO:0000256|RuleBase:RU004996};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152, ECO:0000256|RuleBase:RU004996};
GN Name=tkt {ECO:0000313|EMBL:CAL27891.1};
GN OrderedLocusNames=Sca_0983 {ECO:0000313|EMBL:CAL27891.1};
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513 {ECO:0000313|EMBL:CAL27891.1, ECO:0000313|Proteomes:UP000000444};
RN [1] {ECO:0000313|EMBL:CAL27891.1, ECO:0000313|Proteomes:UP000000444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300 {ECO:0000313|EMBL:CAL27891.1,
RC ECO:0000313|Proteomes:UP000000444};
RX PubMed=19060169; DOI=10.1128/AEM.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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|ARBA:ARBA00002931,
CC 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 -!- PATHWAY: Carbohydrate biosynthesis; Calvin cycle.
CC {ECO:0000256|ARBA:ARBA00005215}.
CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway.
CC {ECO:0000256|ARBA:ARBA00004959}.
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; AM295250; CAL27891.1; -; Genomic_DNA.
DR RefSeq; WP_015900232.1; NC_012121.1.
DR AlphaFoldDB; B9DP72; -.
DR GeneID; 60545325; -.
DR KEGG; sca:SCA_0983; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_9; -.
DR OrthoDB; 8732661at2; -.
DR BioCyc; SCAR396513:SCA_RS04940-MONOMER; -.
DR UniPathway; UPA00115; -.
DR UniPathway; UPA00116; -.
DR Proteomes; UP000000444; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-UniPathway.
DR GO; GO:0019253; P:reductive pentose-phosphate cycle; IEA:UniProtKB-UniPathway.
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|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU004996};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842, ECO:0000256|RuleBase:RU004996};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004996};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 353..524
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 662 AA; 72820 MW; 116592D757995C6C CRC64;
MFDKKDELAV NTIRALSIDA VEKANSGHPG LPMGAAPMAY TLWTRHLNFN PNSNEYFNRD
RFILSAGHGS ALLYSLLHVS GSLELEELKQ FRQWDSKTPG HPEFRHTQGV EVTTGPLGQG
FAMSVGMAMA EDHLAGKFNK PDANVVDHYT YVLASDGDLM EGISHEAASL AGHLQLDKLI
ALYDSNDISL DGDLDKAFSE NIKQRFEAYG WNHILVKDGN DLEEINNAIE EAKKQKGPTM
IEVKTVIGYG SPNKSGTHGV HGAPLGEDER KLTIENYHLD PEKRFYVPDE VYDIFSNTML
KRADENEAAW KKLVEKYSEE YPELADEFKK AINGELPKDY AEHLPEFKVG TESATRADSG
DVIQSLSEHV PSFFGGSADL AGSNKSNVKE AVDYDRNTPE GKNIWFGVRE FAMGAAVNGM
AAHGGLNPYG ATFFVFSDYL KPALRLSAIM GLNSTFIFTH DSIAVGEDGP THEPIEQLAA
LRSLPNMNVI RPADGNETRV AWEVALETEN TPTSLVLTRQ NLPVLDVSKE TVEEGVRKGA
YVVYESDAEP EYLLLATGSE VSLAVEAAKS FAENGKGIRV VSMPNWHAFE QQSKEYKDEI
LPPSITKRLA VEMGATLGWH KYVGLEGEVL GIDRFGASAP GGLVVEKYGF TKENVLKLLN
NL
//
