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Database: UniProt
Entry: Q5QSE4_OENOE
LinkDB: Q5QSE4_OENOE
Original site: Q5QSE4_OENOE 
ID   Q5QSE4_OENOE            Unreviewed;       180 AA.
AC   Q5QSE4;
DT   04-JAN-2005, integrated into UniProtKB/TrEMBL.
DT   04-JAN-2005, sequence version 1.
DT   27-MAR-2024, entry version 44.
DE   SubName: Full=Transketolase {ECO:0000313|EMBL:CAF02259.1};
DE   Flags: Fragment;
GN   Name=recP {ECO:0000313|EMBL:CAF02259.1};
OS   Oenococcus oeni (Leuconostoc oenos).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=1247 {ECO:0000313|EMBL:CAF02259.1};
RN   [1] {ECO:0000313|EMBL:CAF02259.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=15574919; DOI=10.1128/AEM.70.12.7210-7219.2004;
RA   de Las Rivas B., Marcobal A., Munoz R.;
RT   "Allelic diversity and population structure in Oenococcus oeni as
RT   determined from sequence analysis of housekeeping genes.";
RL   Appl. Environ. Microbiol. 70:7210-7219(2004).
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=thiamine diphosphate; Xref=ChEBI:CHEBI:58937;
CC         Evidence={ECO:0000256|ARBA:ARBA00001964};
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DR   EMBL; AJ619672; CAF02259.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q5QSE4; -.
DR   Gene3D; 3.40.50.970; -; 2.
DR   InterPro; IPR029061; THDP-binding.
DR   InterPro; IPR005475; Transketolase-like_Pyr-bd.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF2; TRANSKETOLASE 1-RELATED; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF00456; Transketolase_N; 1.
DR   SUPFAM; SSF52518; Thiamin diphosphate-binding fold (THDP-binding); 2.
PE   4: Predicted;
FT   DOMAIN          1..68
FT                   /note="Transketolase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00456"
FT   DOMAIN          87..180
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|Pfam:PF02779"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:CAF02259.1"
FT   NON_TER         180
FT                   /evidence="ECO:0000313|EMBL:CAF02259.1"
SQ   SEQUENCE   180 AA;  20441 MW;  6899CA394ADE9C47 CRC64;
     HGAAIGEENV AKTRDFYHWS YQPFEIPKDV YDLFNDSHQA KDQYYKSWQE SFELYAKAFP
     QLAEQLKNND STLNTANLKL AENNGQELAT RVSSSEVMQQ IADQNRTFWG GSADLSSSNK
     TYLKDQGDFT DLTPQGSNVF YGVREFTMAA ITNGILLHGN SRAFASTFFI FSDYMKPAIR
//
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