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Database: UniProt
Entry: A0A2N5I4C3_9BACI
LinkDB: A0A2N5I4C3_9BACI
Original site: A0A2N5I4C3_9BACI 
ID   A0A2N5I4C3_9BACI        Unreviewed;       668 AA.
AC   A0A2N5I4C3;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   24-JAN-2024, entry version 19.
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:PLS16780.1};
GN   ORFNames=CVD28_17050 {ECO:0000313|EMBL:PLS16780.1};
OS   Bacillus sp. M6-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2054166 {ECO:0000313|EMBL:PLS16780.1, ECO:0000313|Proteomes:UP000234907};
RN   [1] {ECO:0000313|EMBL:PLS16780.1, ECO:0000313|Proteomes:UP000234907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M6-12 {ECO:0000313|EMBL:PLS16780.1,
RC   ECO:0000313|Proteomes:UP000234907};
RA   Seuylemezian A., Cooper K., Vaishampayan P.;
RT   "Comparitive Functional Genomics of Dry Heat Resistant strains isolated
RT   from the Viking Spacecraft.";
RL   Submitted (NOV-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:PLS16780.1}.
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DR   EMBL; PGVF01000014; PLS16780.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2N5I4C3; -.
DR   OrthoDB; 8732661at2; -.
DR   Proteomes; UP000234907; 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; 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          14..34
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   668 AA;  72238 MW;  6B1F6784B8355C2C CRC64;
     MLNKIDDLSI ATIRTLSIDA IEKANSGHPG LPMGAAPMAY TLWTRFLNHN PQNPAWFNRD
     RFVLSAGHGS MLLYSLLHLS GYGVGMDDIK NFRQWGSKTP GHPEYGHTPG VDATTGPLGQ
     GIAMAVGMAM AERHLAATYN TNDYNVVDHF TYSICGDGDL QEGVSAEAAS LAGHLKLGKL
     IVLYDSNDIT LDGELNKSFS ESVAERFKAY GWNYIRVENG NDISEVANAI EKAKSDTSRP
     TLIEVKTIIG YGSPNRSGTS SVHGAPLGED EMKLTKEFYN WTFDQDFHVP EEVYAHFKET
     VAESGSKKEE EWNSLFNQYK EANPKLGEQL EAAINGQLPE GWDKDIPVYE EGKSVASRAS
     SGEVLNAIAK NLPSFFGGSA DLAGSNKTDI KGAGDFLPGD YSGRNIWFGV REFAMGAALN
     GMALHGGLNV FAGTFFVFSD YLRPAIRLAA LMNLPVTYVF THDSIAVGED GPTHEPVEQL
     PALRAMPNLS VIRPADGNET AAAWKAALES KDRPTALVLT RQNLPTLAST AEKAYEGVSK
     GAYIVSASGK EQPDALLLAS GSEVNLAVDA QKALSAEGID VSVISMPAWD RFEEQSKEYK
     QSVISPAVKK RLAIEMAAPL GWDRYTGDEG DILAINTFGA SAPGEKIMEE YGFTVQNVVS
     RVKALLNN
//
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