ID   J2Z641_9LACO            Unreviewed;       677 AA.
AC   J2Z641;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   ORFNames=A11Y_119202 {ECO:0000313|EMBL:EJN56013.1};
OS   Loigolactobacillus coryniformis subsp. coryniformis CECT 5711.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Loigolactobacillus.
OX   NCBI_TaxID=1185325 {ECO:0000313|EMBL:EJN56013.1, ECO:0000313|Proteomes:UP000007271};
RN   [1] {ECO:0000313|EMBL:EJN56013.1, ECO:0000313|Proteomes:UP000007271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CECT5711 {ECO:0000313|Proteomes:UP000007271};
RA   Rodriguez J.M.;
RT   "Complete Genome Sequence of Lactobacillus coryniformis CECT5711.";
RL   Submitted (MAY-2012) 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:EJN56013.1}.
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DR   EMBL; AKFP01000023; EJN56013.1; -; Genomic_DNA.
DR   RefSeq; WP_003678329.1; NZ_AKFP01000023.1.
DR   AlphaFoldDB; J2Z641; -.
DR   STRING; 1185325.A11Y_119202; -.
DR   PATRIC; fig|1185325.3.peg.1188; -.
DR   Proteomes; UP000007271; 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.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007271}.
FT   DOMAIN          352..523
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   677 AA;  73040 MW;  7A7B2FF562D02386 CRC64;
     MFDETDQLSV NALRALSIDM IERAGSGHPG LPLDAAPMAY VLYSRHLRVD PQAPDWVNRD
     RFVLSAGHGS ALLYSMLHLS GFPTRMADLK QFRQLHSMTP GHPEHGLVAG VDATTGPLGQ
     GLGMAVGMAM AETHLAAQYN TPEQKVIDHF TYVICGDGDL MEGISHEAAS LAGNLKLNKL
     IVLYDSNDVS LDGATDRTFS DDAQQRFAGY GWDCQKVSDG NNLAAIDAAI TAAKLTDAPS
     MIEIKTTIGY GAPKQGTHLV HGAPLGQTDL AATKQSLGWQ AAPFTVPAAV KQRFAERVQE
     RGQAAHRQWQ ALLTTYQQAQ PKLAAQLHHA LAQELPVDWQ SDLPKYQIGD SEAGRITSQK
     MIQALAAKVP SLWGGAADLA SSNKTDIAAS GSFSATARQE RNLNFGVREF AEAAAMNGIA
     LHGGSHVFGG TFFVFSDYMR GAIRLAALQK LPVTYIFTHD SLAVGEDGPT HEPVEQLMSL
     RAMPGISVIR PADPNEAVAA WRLAMTTNDR PSVLVLTRQD LAVLKGSLNH PDGVSRGGYV
     ISPQQRKQAE GILLASGSEV ALVIAAQQRL RKFGHDVAVV SMPCFDRFMQ QPAAYREKVL
     PRNIRRRVSI ELGATLGWER FIGLDGLSLG IDTFGASGPA AEVLAEYGFT SDAVVAAYQK
     LWRADNRLQT PIRRSVI
//