GenomeNet

Database: UniProt
Entry: Q04DY2_OENOB
LinkDB: Q04DY2_OENOB
Original site: Q04DY2_OENOB 
ID   Q04DY2_OENOB            Unreviewed;       679 AA.
AC   Q04DY2;
DT   14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE            EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN   OrderedLocusNames=OEOE_1480 {ECO:0000313|EMBL:ABJ57340.1};
OS   Oenococcus oeni (strain ATCC BAA-331 / PSU-1).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Oenococcus.
OX   NCBI_TaxID=203123 {ECO:0000313|EMBL:ABJ57340.1, ECO:0000313|Proteomes:UP000000774};
RN   [1] {ECO:0000313|EMBL:ABJ57340.1, ECO:0000313|Proteomes:UP000000774}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-331 / PSU-1 {ECO:0000313|Proteomes:UP000000774};
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA   Kozyavkin S., Weimer B., Mills D.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000411; ABJ57340.1; -; Genomic_DNA.
DR   RefSeq; WP_002821710.1; NC_008528.1.
DR   AlphaFoldDB; Q04DY2; -.
DR   STRING; 203123.OEOE_1480; -.
DR   KEGG; ooe:OEOE_1480; -.
DR   PATRIC; fig|203123.7.peg.1499; -.
DR   eggNOG; COG0021; Bacteria.
DR   HOGENOM; CLU_009227_0_0_9; -.
DR   Proteomes; UP000000774; Chromosome.
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:UP000000774};
KW   Transferase {ECO:0000313|EMBL:ABJ57340.1}.
FT   DOMAIN          361..532
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   679 AA;  75726 MW;  C1E57442B3F26D1E CRC64;
     MIDTQFENIP LKELNRQDEQ QAVNAIRFLS LDMIQKANSG HPGLPLDAAP MAYTLFQKFL
     NFNNRDPYWI NRDRFVLSAG HGSALLYSLL HLNGFKVGID DLKRFRQLDS LTPGHPEWKH
     TPGIDATTGP LGQGLTMAVG MAMAEKHLSA IYNRPGFNIF DHETYVIVGD GDLMEGISQE
     SMAIAGEKRL SKLIVLFDSN DVSLDGSLKL STGEKIQDRI IGNGWDYQFV ADGNNLSDID
     EAIREAKKSD KPSFIEIKTI IGYGTPLQGS SKVHGAAIGE ENVAKTRDFY HWPYQPFEIP
     KDVYDLFNDS HQAKDRYYKS WQESFQLYAE AFPRLAEQLE NNDSTLNTDN LKLAENNDQE
     LATRVSSSEV MQQIADQNRT FWGGSADLSS SNKTYLKDQG DFTDLTPQGS NVFYGVREFA
     MAAITNGILL HGNSRAFAST FFIFSDYMKP AIRLAALQKL ASIFIFSHDS LAVGEDGPTH
     QPVEQLETLR TTPGIDVYRP ADQNETLAAW KAIAKTTNRP TALVTSRQKL PVLRETKDAP
     VERGAYIVSS AKKDLPDAIL IASGSELHLA LEAKRELEKE GYDLSVVSMP SMEAFQRQSE
     EYQASVLPKQ VVNRLSIEMA SSLAWGRYTG IFGKNLAVDT FGKSGKANDV IDDYGFNLAH
     ISRMVKKMID ENKNLQIVK
//
DBGET integrated database retrieval system