ID A0A2K3P8S2_TRIPR Unreviewed; 738 AA.
AC A0A2K3P8S2;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=transketolase {ECO:0000256|ARBA:ARBA00013152};
DE EC=2.2.1.1 {ECO:0000256|ARBA:ARBA00013152};
GN ORFNames=L195_g008303 {ECO:0000313|EMBL:PNY11691.1};
OS Trifolium pratense (Red clover).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; Hologalegina; IRL clade; Trifolieae; Trifolium.
OX NCBI_TaxID=57577 {ECO:0000313|EMBL:PNY11691.1, ECO:0000313|Proteomes:UP000236291};
RN [1] {ECO:0000313|EMBL:PNY11691.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY11691.1};
RX PubMed=24500806; DOI=10.3732/ajb.1300340;
RA Istvanek J., Jaros M., Krenek A., Repkova J.;
RT "Genome assembly and annotation for red clover (Trifolium pratense;
RT Fabaceae).";
RL Am. J. Bot. 101:327-337(2014).
RN [2] {ECO:0000313|EMBL:PNY11691.1, ECO:0000313|Proteomes:UP000236291}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Tatra {ECO:0000313|Proteomes:UP000236291};
RC TISSUE=Young leaves {ECO:0000313|EMBL:PNY11691.1};
RX PubMed=28382043; DOI=10.3389/fpls.2017.00367;
RA Istvanek J., Dluhosova J., Dluhos P., Patkova L., Nedelnik J., Repkova J.;
RT "Gene Classification and Mining of Molecular Markers Useful in Red Clover
RT (Trifolium pratense) Breeding.";
RL Front. Plant Sci. 8:367-367(2017).
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=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 -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
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:PNY11691.1}.
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DR EMBL; ASHM01004717; PNY11691.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2K3P8S2; -.
DR STRING; 57577.A0A2K3P8S2; -.
DR Proteomes; UP000236291; 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; IPR020826; Transketolase_BS.
DR InterPro; IPR033248; Transketolase_C.
DR InterPro; IPR049557; Transketolase_CS.
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.
DR PROSITE; PS00802; TRANSKETOLASE_2; 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:UP000236291};
KW Thiamine pyrophosphate {ECO:0000256|ARBA:ARBA00023052};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 428..600
FT /note="Transketolase-like pyrimidine-binding"
FT /evidence="ECO:0000259|SMART:SM00861"
FT REGION 1..51
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 79813 MW; AF5927CF769ACAD7 CRC64;
MASSSSCTSL SLTNPHLTPT TTTTTRLSSL PSTISLTRSP TPTRLSLSQS QTHLRHITIP
HASSTPAVTP TTETTTLVEK SVNTIRFLAI DSVEKANSGH PGLPMGCAPM GHVLYDEVMR
YNPKNPFWFN RDRFVLSAGH GCMLQYALLH LAGYDSVKEQ DLKEFRQWGS RTPGHPENFE
TPGIEVTTGP LGQGIANAVG LALAEKHLAA RFNKPDNEII DHYTYCILGD GCQMEGIANE
AASLAGHWGL GKLIAFYDDN HISIDGDTEI AFTESVEKRF EGLGWHVIWV QNGNTGFDEI
RAAIKEAKAV KDRPTLIKFT TTIGYGSPNK SNSYSVHGSA LGAKEVDATR NNLGWPYEPF
HVPEDVKKHW SRHIPEGAAL ESEWNAKFAA YEKKYKEEAA VLKSIISGEL PSGWEKALPT
YTPEIPADAT RNLSQTNLNA LAKVLPGLLG GSADLASSNM TLLKAFGNFQ SGTPEERNVR
FGVREHGMGA ICNGIALHSP GLIPYCATFF VFTDYMRGAI RLSALSEAGV IYVMTHDSIG
LGEDGPTHQP IEHLASFRAM PNILMLRPAD GNETAGAYKV AVLNRKRPSI LALSRQKLPN
LPGTSIEGVG KGGYIVSDNS TGNKPDVILI GTGSELEIAY YAAEDLRKEG KAVRVVSFVS
WELFDEQSDA YKESVLPGAV SARVSIEAGS TFGWEKIVGS KGKAIGIDRF GASAPAGRIY
KEFGITKEAV IAAAKELI
//
