ID A0A220U636_9BACI Unreviewed; 667 AA.
AC A0A220U636;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:ASK63442.1};
GN ORFNames=CFK37_15400 {ECO:0000313|EMBL:ASK63442.1};
OS Virgibacillus phasianinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=2017483 {ECO:0000313|EMBL:ASK63442.1, ECO:0000313|Proteomes:UP000198312};
RN [1] {ECO:0000313|EMBL:ASK63442.1, ECO:0000313|Proteomes:UP000198312}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LM2416 {ECO:0000313|EMBL:ASK63442.1,
RC ECO:0000313|Proteomes:UP000198312};
RA Tak E.J., Bae J.-W.;
RT "Virgibacillus sp. LM2416.";
RL Submitted (JUL-2017) 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; CP022315; ASK63442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A220U636; -.
DR KEGG; vil:CFK37_15400; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000198312; 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:UP000198312};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052,
KW ECO:0000256|RuleBase:RU004996};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004996}.
FT DOMAIN 355..526
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
SQ SEQUENCE 667 AA; 73081 MW; AAE194A98649A65A CRC64;
MSSNVEELSI NTIRTLAIDA IENANSGHPG LPMGAAPMAY TLWTDFMNQN PKNSKWFNRD
RFVLSAGHGS MLLYGLLHLA GYDVTIEDLK NFRQWDSKTP GHPEVHHTDG VEATTGPLGQ
GIAMAVGMAM AEAHLGATFN KEDLSIVDHH TYALISDGDL MEGISHETAS LAGHLGLGKL
IALYDSNDIS LDGDLDRSFS DDTELRFKAY GWQVIRVEDG NDVKALRNAI KEAKENTSQP
TLIEVKTVIG FGSPNKSASS ASHGAPLGVD EVKLTKESYK WTHDDFHVPE EVYADFNEKI
GKNGQDVEDN WNQLFDNYKE KYPEDAEKLE QAINGELPLD WNEELPLYEP GKDKLATRAS
SGEVLNAVSN AVPNLFGGSA DLAGSNKTTV KNQTDFSLDN YAGKNIWFGV REFAMAAALN
GMALHGGLKV YAGTFFVFSD YLRPAVRLSA IMNNPVTYVF THDSIAVGED GPTHEPIEHL
PAFRAMPGLS LIRPADGNET QAAWRLALES TNKPTALVLT RQGLPTLEGT KENAYEGVKK
GAYVISKSEK ETPDALILAT GSEVQLAVRA QKELLEKDIH VNVVSMPSWD RFNEQEAAYR
NEVIPPQVKS RLAIEMASPF GWERYVGDQG TVLGIDTFGA SANGDKVMEE YGFTVENVVK
QVEKLIK
//
