ID A0A0W7YJU3_9BACI Unreviewed; 664 AA.
AC A0A0W7YJU3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 27.
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 ORFNames=AK833_08495 {ECO:0000313|EMBL:KUF35044.1};
OS Lysinibacillus sp. F5.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX NCBI_TaxID=1700846 {ECO:0000313|EMBL:KUF35044.1, ECO:0000313|Proteomes:UP000053086};
RN [1] {ECO:0000313|EMBL:KUF35044.1, ECO:0000313|Proteomes:UP000053086}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F5 {ECO:0000313|EMBL:KUF35044.1,
RC ECO:0000313|Proteomes:UP000053086};
RA Chan X.Y., Chan K.G., Hong K.W., Tan A., Chen J.W.;
RT "Draft Genome of marine Lysinibacillus sp. F5.";
RL Submitted (OCT-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUF35044.1}.
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DR EMBL; LKIE01000043; KUF35044.1; -; Genomic_DNA.
DR RefSeq; WP_058843965.1; NZ_LKIE01000043.1.
DR AlphaFoldDB; A0A0W7YJU3; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000053086; 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; 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 Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 354..525
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 664 AA; 71114 MW; A3259FF94A281F6D CRC64;
MTQHADLLAI NAIRTLSIDA IEKANSGHPG LPMGAAPMAY TLWTKQLRHN PANPKWYNRD
RFVLSAGHGS MLLYSLLHLG GYGLPMEEIQ NFRQWDSLTP GHPEYGHTVG VEATTGPLGQ
GIAMTVGMAM AERHLAATYN KPGHDIVDHY TFALCGDGDL MEGVAAEAIS LAGHLKLEKL
IVLYDSNDIS LDGDLEKSFS ENVQKRFESY GWNYLKVADG TDVDAINATI EEAKKSTGKP
TLIEVKTVIG FGSPNKSGKA DSHGAPLGTD EVVLTKAAYE WAHEPFQIPA EVYDTFNAAA
EIQGAQSEEA WNAKFAAYKE EFPELAAQFE KAMNGELPED FASELPVYEA GKSVATRSSS
GDAINAIAKK TPSFFGGSAD LAGSNKTTMK GAGDFSADDY AGRNIWFGVR EFAMGAAMNG
MALHGGLNVF GGTFFVFSDY VRPAVRLSAL MGLPVTYVFT HDSIAVGEDG PTHEPIEHLA
SLRAMPNLSV IRPADANESA VAWELAVASE KTPTVLVLSR QNLPVLDASI ETVRDGVTKG
AYTVSPATKE VADAILIATG SEVSLAVEAQ KALKAEGVDV AVVSMPSMDR FEKQDAAYKE
SVLPKAVTKR LAIEMGASFG WHKYTGFEGD VLAIDKFGAS APGELVMEKY GFTVENVVAK
VKAL
//
