ID Q8KBB9_CHLTE Unreviewed; 688 AA.
AC Q8KBB9;
DT 01-OCT-2002, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2002, sequence version 1.
DT 27-MAR-2024, entry version 136.
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 Name=tkt {ECO:0000313|EMBL:AAM73089.1};
GN OrderedLocusNames=CT1870 {ECO:0000313|EMBL:AAM73089.1};
OS Chlorobaculum tepidum (strain ATCC 49652 / DSM 12025 / NBRC 103806 / TLS)
OS (Chlorobium tepidum).
OC Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chlorobiaceae;
OC Chlorobaculum.
OX NCBI_TaxID=194439 {ECO:0000313|EMBL:AAM73089.1, ECO:0000313|Proteomes:UP000001007};
RN [1] {ECO:0000313|EMBL:AAM73089.1, ECO:0000313|Proteomes:UP000001007}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49652 / DSM 12025 / NBRC 103806 / TLS
RC {ECO:0000313|Proteomes:UP000001007};
RX PubMed=12093901; DOI=10.1073/pnas.132181499;
RA Eisen J.A., Nelson K.E., Paulsen I.T., Heidelberg J.F., Wu M., Dodson R.J.,
RA Deboy R., Gwinn M.L., Nelson W.C., Haft D.H., Hickey E.K., Peterson J.D.,
RA Durkin A.S., Kolonay J.L., Yang F., Holt I., Umayam L.A., Mason T.,
RA Brenner M., Shea T.P., Parksey D., Nierman W.C., Feldblyum T.V.,
RA Hansen C.L., Craven M.B., Radune D., Vamathevan J., Khouri H., White O.,
RA Gruber T.M., Ketchum K.A., Venter J.C., Tettelin H., Bryant D.A.,
RA Fraser C.M.;
RT "The complete genome sequence of Chlorobium tepidum TLS, a photosynthetic,
RT anaerobic, green-sulfur bacterium.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:9509-9514(2002).
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; AE006470; AAM73089.1; -; Genomic_DNA.
DR RefSeq; NP_662747.1; NC_002932.3.
DR AlphaFoldDB; Q8KBB9; -.
DR STRING; 194439.CT1870; -.
DR EnsemblBacteria; AAM73089; AAM73089; CT1870.
DR KEGG; cte:CT1870; -.
DR PATRIC; fig|194439.7.peg.1696; -.
DR eggNOG; COG0021; Bacteria.
DR HOGENOM; CLU_009227_0_0_10; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000001007; Chromosome.
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; 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:UP000001007};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 373..541
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 688 AA; 74373 MW; 9FC8909355F4D0FF CRC64;
MTVRVRPISL NLRNNPIMTR TRSIDEEAVA TIRLLAVDMV EKAKSGHPGL PLGAAPMAYT
LFTKIMRFNP ANPEWPNRDR FVLSAGHGSA LLYSMLHLCG YGLGMDELKQ FRQLGSRTPG
HPEYGHTPGV ETTTGPLGQG IATAVGMAAA ERFLATKLNT AERALIDHFT YVICGDGDLM
EGISSEASSL AGHLRLGRLI CLYDSNHISI EGSTGLAFTE DVARRYEAYG WHVLSHIDGN
DLAAIEQAVR NAQEIDDRPS LIIVNTTIGY GSPHKQGTAS AHGEPLGPEE TKLVKQAFGF
DENESFVVSD RVYDHFHAIA ERGAALEAEW QTQWQSFRQE EPGLASALTD LLAGRFPESW
LPEMPKFTTG EKLATRQASK SVLAKIAEKA PLLAGGSADL APSNGTLIGA AFEAGSYGGS
TFHFGVREHA MGALVNGMAL SKMMIPYGAT FLVFADYMKP ALRIAAMMQS PSIFIFTHDS
IGLGEDGPTH QPIEQLAMLR AMPGFDVYRP ADANETAAAW LLALKRRKPA ALVLTRQGLP
VLDDADGRLR NGVTKGGYVL AEWADTDDDD DRRIIIVATG SEVHPALEAK TLIEQEGFAA
RVVSMPSREL FAEQPAEYRA AVLPPTVRAR AVVEAAATFG WHDIAGDGGI VIGIDRFGMS
APSSQVMEHF GFTAENIAAR ALELLNRK
//
