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
//