ID A0A235FC35_9BACI Unreviewed; 666 AA.
AC A0A235FC35;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
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:OYD58759.1};
GN ORFNames=CGZ90_02335 {ECO:0000313|EMBL:OYD58759.1};
OS Fictibacillus aquaticus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=2021314 {ECO:0000313|EMBL:OYD58759.1, ECO:0000313|Proteomes:UP000215059};
RN [1] {ECO:0000313|EMBL:OYD58759.1, ECO:0000313|Proteomes:UP000215059}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GDSW-R2A3 {ECO:0000313|EMBL:OYD58759.1,
RC ECO:0000313|Proteomes:UP000215059};
RA Mayilraj S.;
RT "Fictibacillus sp. nov. GDSW-R2A3 Genome sequencing and assembly.";
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}.
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:OYD58759.1}.
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DR EMBL; NOII01000001; OYD58759.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A235FC35; -.
DR OrthoDB; 8732661at2; -.
DR Proteomes; UP000215059; 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 Reference proteome {ECO:0000313|Proteomes:UP000215059};
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 666 AA; 72443 MW; B5F42002708F046D CRC64;
MIGLARTIDQ LSINTIRTLS IDSIEKANSG HPGMPMGAAP MAYSLWTKFM NHNPGNPEWF
NRDRFVLSAG HGSMLLYSLL HLSGYGLTLD DLKQFRQWGS KTPGHPEYKH TPGVEATTGP
LGQGLAMAVG MAMAERHLAA KYNRDELNVI DHYTYSICGD GDLMEGISSE AASLAGHLAL
GRLVVLYDSN DISLDGDLHH SFSENVQKRF EAYGWQVLFV EDGTDLDSIE KAIEAAKADT
SKPTLIEVKT VIGHGSPNKS GKSASHGAPL GVDEIKLTKE AYKWTFEEDF HVPSEVSDHF
SSLKEQGQKK EQEWEELFKT YKEKYPELAA ELKNAISGKL PENWDAEMPE FEKATATRAT
SGAAINALSK SVPALFGGSA DLAGSNHTLV KGENNFSRND YSGRNIWFGV REFGMAAALN
GMALHGGLKV YGGTFFVFSD YLRPAVRLSA LMGLPVTYVL THDSVAVGED GPTHEPVEQL
SSLRAMPNLH VVRPADGYES NAAWKLALES TDQPTVMVLS RQNLPILKST KEQAYEGVKR
GAYVVSPSEG TADVLLLASG SEVSLAVEAQ ELLKQEGINA SVVSMPSWDR FEKQDAGYKE
EVLPSDVKVR LGIEMGSSLG WHKYVGDAGD VLAIDSFGAS APGETIMKEY GFTAENVVNR
VKALMK
//
