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Database: UniProt
Entry: A0A0M2PEE6_9BACI
LinkDB: A0A0M2PEE6_9BACI
Original site: A0A0M2PEE6_9BACI 
ID   A0A0M2PEE6_9BACI        Unreviewed;       680 AA.
AC   A0A0M2PEE6;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 30.
DE   RecName: Full=Transketolase {ECO:0000256|ARBA:ARBA00016662};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=WQ54_16145 {ECO:0000313|EMBL:KKI91205.1};
OS   Bacillus sp. SA1-12.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1455638 {ECO:0000313|EMBL:KKI91205.1, ECO:0000313|Proteomes:UP000034887};
RN   [1] {ECO:0000313|EMBL:KKI91205.1, ECO:0000313|Proteomes:UP000034887}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA1-12 {ECO:0000313|EMBL:KKI91205.1,
RC   ECO:0000313|Proteomes:UP000034887};
RA   Kumar A., Mathan Kumar R., Kaur N., Kumar N., Singh N.K., Kaur G.,
RA   Mayilraj S.;
RT   "Taxonomic description and genome sequence of Bacillus tuticoriensis sp.
RT   nov., a novel member of the genus Bacillus isolated from solar saltern.";
RL   Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000256|ARBA:ARBA00001946};
CC   -!- COFACTOR:
CC       Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
CC   -!- SIMILARITY: Belongs to the transketolase family.
CC       {ECO:0000256|ARBA:ARBA00007131}.
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:KKI91205.1}.
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DR   EMBL; LATZ01000034; KKI91205.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0M2PEE6; -.
DR   PATRIC; fig|1455638.3.peg.3589; -.
DR   Proteomes; UP000034887; 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; 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.
PE   3: Inferred from homology;
KW   Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000034887};
KW   Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          18..38
FT                   /note="Transketolase signature 1"
FT                   /evidence="ECO:0000259|PROSITE:PS00801"
SQ   SEQUENCE   680 AA;  74334 MW;  34CF715575AA33C5 CRC64;
     MKGKKTMNIE TLAVNTIRTL SIDAINCANS GHPGLPMGAA PMAYALWANH LQHSPENSKW
     FNRDRFVLSA GHGSSLLYSL LHLAGYDVSL EDLKSFRKLN SKTPGHPEFG HTDGVEVTTG
     PLGQGISNAV GMAMAEAHLA AKFNQDGFSV IDHYTYALVG DGDLMEGISY EAMSLAGHMN
     LGKLVVLYDS NDISLDGSLN LSFSEDIQKR VESAKWQYLR VEDGNSVADI TNAIELAKLN
     TDQPTLIEIR TIIGYGSPKV AGTNKAHGNP LGAEEAAATK QAYGWHYEED FFVPEEVKAH
     FEELKQRGMV KEQQWNDLFH SYREAYPSLA RELEGAIKGE AIVQDQDILT FDTEKAVSTR
     VASGEAINHY AKIIPAIFGG SADLSHSTMT DMKDEAVYAV ESFAGRNVYF GVREHAMGAA
     GNGIALHGGL KPFVSTFFVF NDYLRPSIRL AALQKLPITY VFTHDSIAVG EDGPTHEPIE
     HLVSLRAIPG LTVIRPTDAN ETASAWAYAL QQTDGPVALV LSRQNLPVFE ETKANIENLS
     KGAYVLTQTD ENPDVILLAT GSEVSLAVEA KAELEKEEIS VRVVAMPSWE LFNSQSNEYK
     EYVLPSSVSN RVALEMGISL GWERFIGPKG KVLSIETFGA SGTGAEVMEL FGFTVKNVVE
     ITRNLFNSEK QEEFGYETIH
//
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