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Database: UniProt
Entry: F6HNF2_VITVI
LinkDB: F6HNF2_VITVI
Original site: F6HNF2_VITVI 
ID   F6HNF2_VITVI            Unreviewed;       636 AA.
AC   F6HNF2;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=Transketolase-like pyrimidine-binding domain-containing protein {ECO:0000259|SMART:SM00861};
GN   OrderedLocusNames=VIT_13s0019g04500 {ECO:0000313|EMBL:CCB56171.1};
OS   Vitis vinifera (Grape).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; Vitales; Vitaceae; Viteae; Vitis.
OX   NCBI_TaxID=29760 {ECO:0000313|EMBL:CCB56171.1, ECO:0000313|Proteomes:UP000009183};
RN   [1] {ECO:0000313|Proteomes:UP000009183}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Pinot noir / PN40024 {ECO:0000313|Proteomes:UP000009183};
RX   PubMed=17721507; DOI=10.1038/nature06148;
RG   The French-Italian Public Consortium for Grapevine Genome Characterization.;
RA   Jaillon O., Aury J.-M., Noel B., Policriti A., Clepet C., Casagrande A.,
RA   Choisne N., Aubourg S., Vitulo N., Jubin C., Vezzi A., Legeai F.,
RA   Hugueney P., Dasilva C., Horner D., Mica E., Jublot D., Poulain J.,
RA   Bruyere C., Billault A., Segurens B., Gouyvenoux M., Ugarte E.,
RA   Cattonaro F., Anthouard V., Vico V., Del Fabbro C., Alaux M.,
RA   Di Gaspero G., Dumas V., Felice N., Paillard S., Juman I., Moroldo M.,
RA   Scalabrin S., Canaguier A., Le Clainche I., Malacrida G., Durand E.,
RA   Pesole G., Laucou V., Chatelet P., Merdinoglu D., Delledonne M.,
RA   Pezzotti M., Lecharny A., Scarpelli C., Artiguenave F., Pe M.E., Valle G.,
RA   Morgante M., Caboche M., Adam-Blondon A.-F., Weissenbach J., Quetier F.,
RA   Wincker P.;
RT   "The grapevine genome sequence suggests ancestral hexaploidization in major
RT   angiosperm phyla.";
RL   Nature 449:463-467(2007).
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000256|ARBA:ARBA00001941};
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}.
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DR   EMBL; FN595998; CCB56171.1; -; Genomic_DNA.
DR   AlphaFoldDB; F6HNF2; -.
DR   STRING; 29760.F6HNF2; -.
DR   PaxDb; 29760-VIT_13s0019g04500-t01; -.
DR   EnsemblPlants; Vitvi13g04177_t001; Vitvi13g04177_P001; Vitvi13g04177.
DR   Gramene; Vitvi13g04177_t001; Vitvi13g04177_P001; Vitvi13g04177.
DR   eggNOG; KOG0523; Eukaryota.
DR   HOGENOM; CLU_009227_0_0_1; -.
DR   InParanoid; F6HNF2; -.
DR   Proteomes; UP000009183; Chromosome 13.
DR   ExpressionAtlas; F6HNF2; baseline and differential.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004802; F:transketolase activity; IBA:GO_Central.
DR   GO; GO:0006098; P:pentose-phosphate shunt; IBA:GO_Central.
DR   CDD; cd07033; TPP_PYR_DXS_TK_like; 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; IPR033248; Transketolase_C.
DR   InterPro; IPR033247; Transketolase_fam.
DR   InterPro; IPR005474; Transketolase_N.
DR   PANTHER; PTHR43522; TRANSKETOLASE; 1.
DR   PANTHER; PTHR43522:SF5; TRANSKETOLASE; 1.
DR   Pfam; PF02779; Transket_pyr; 1.
DR   Pfam; PF02780; Transketolase_C; 1.
DR   Pfam; PF00456; Transketolase_N; 2.
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:UP000009183}.
FT   DOMAIN          321..495
FT                   /note="Transketolase-like pyrimidine-binding"
FT                   /evidence="ECO:0000259|SMART:SM00861"
SQ   SEQUENCE   636 AA;  70610 MW;  B1C972131F67ADFB CRC64;
     MLIVDAVQTA KAGHSGMPLG MAKVGYILYR HVMRYNPRNP KWFNRDRFVL SAGHGCLLQY
     ICLHLAGFQS VQLEDLQRLC LVVGPQVTLR MWLPMALKSL QAPWARFNKP DAVIVDHRTF
     CIMGDGCVME GISHEAASLA AHWKLNKLTL IYDDNLNTID GATSLAFSED ISARFKALRW
     NTITVDDTHN DMEAIKNALL SAFRETEKPT FIRVCKLSEK KGISKAHHGT FDEKDVKKMR
     RKVSWSDREP FHVIPMIYRL VFKSAAGKCR YKQSMEWHSR LCYYQTKYPQ EFVEFKILLD
     GGLLPGWESS LPKFPTSDPV DATQGYSEKC LSQLAKVLPG LIRGSADLAT SNKAYLHGHE
     DFSQPNSPWG CNIRYGVREH AMAGISNGIA LHGSGLIPFA ATFLVFSDYM KNSIRLSALS
     HAGVIYIMTH DSIGLGEDGP THQPAVEQLA GLRAVPQLLV FRPADGNETA GAYKVAVANR
     NVPSLIALSR QKVAANLEGT SRASVERGGY IVSDNSEDKL PDIILIGTGS ELCLCDEGAK
     MLRQEGRTVR VVSLVCWRLF DMQPQQYKEF VLPPSVSKRV SVEAASPIGW REYVGEEGVV
     VGVEEFGASG AYLDTFKKFG FTEGNITRIA KSLLSQ
//
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