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Protein

Transketolase-2, chloroplastic

Gene

TKL-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the reversible transfer of a two-carbon ketol group from fructose-6-phosphate or sedoheptulose-7-phosphate to glyceraldehyde-3-phosphate to yield xylulose-5-phosphate and erythrose-4-phosphate or ribose-5-phosphate, respectively (By similarity). Could act as a stress sensor involved in adaptation process.By similarity1 Publication

Catalytic activityi

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Ca2+By similarity, Mn2+By similarity, Co2+By similarityNote: Binds 1 Mg2+ ion per subunit. Can also utilize other divalent metal cations, such as Ca2+, Mn2+ and Co2+.By similarity
  • thiamine diphosphateBy similarityNote: Binds 1 thiamine pyrophosphate per subunit.By similarity

Pathwayi: Calvin cycle

This protein is involved in the pathway Calvin cycle, which is part of Carbohydrate biosynthesis.
View all proteins of this organism that are known to be involved in the pathway Calvin cycle and in Carbohydrate biosynthesis.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei103SubstrateBy similarity1
Sitei103Important for catalytic activityBy similarity1
Binding sitei143Thiamine pyrophosphateBy similarity1
Metal bindingi233MagnesiumBy similarity1
Binding sitei234Thiamine pyrophosphate; via amide nitrogenBy similarity1
Metal bindingi263MagnesiumBy similarity1
Binding sitei263Thiamine pyrophosphateBy similarity1
Metal bindingi265Magnesium; via carbonyl oxygenBy similarity1
Binding sitei340SubstrateBy similarity1
Binding sitei340Thiamine pyrophosphateBy similarity1
Sitei340Important for catalytic activityBy similarity1
Binding sitei434SubstrateBy similarity1
Binding sitei461SubstrateBy similarity1
Active sitei488Proton donorBy similarity1
Binding sitei488Thiamine pyrophosphateBy similarity1
Binding sitei515Thiamine pyrophosphateBy similarity1
Binding sitei539SubstrateBy similarity1
Binding sitei547SubstrateBy similarity1
Binding sitei598SubstrateBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi192 – 194Thiamine pyrophosphateBy similarity3

GO - Molecular functioni

GO - Biological processi

  • reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
  • response to cadmium ion Source: TAIR

Keywordsi

Molecular functionTransferase
LigandCalcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

BioCyciARA:AT2G45290-MONOMER
ReactomeiR-ATH-163754 Insulin effects increased synthesis of Xylulose-5-Phosphate
R-ATH-71336 Pentose phosphate pathway (hexose monophosphate shunt)
UniPathwayiUPA00116

Names & Taxonomyi

Protein namesi
Recommended name:
Transketolase-2, chloroplastic (EC:2.2.1.1)
Short name:
TK
Gene namesi
Name:TKL-2
Ordered Locus Names:At2g45290
ORF Names:F4L23.20
OrganismiArabidopsis thaliana (Mouse-ear cress)
Taxonomic identifieri3702 [NCBI]
Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaerosidsmalvidsBrassicalesBrassicaceaeCamelineaeArabidopsis
Proteomesi
  • UP000006548 Componenti: Chromosome 2

Organism-specific databases

AraportiAT2G45290
TAIRilocus:2050837 AT2G45290

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Chloroplast Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertion Graphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Transit peptidei1 – 65ChloroplastSequence analysisCombined sourcesAdd BLAST65
ChainiPRO_000042181866 – 741Transketolase-2, chloroplasticAdd BLAST676

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei66N-acetylalanineCombined sources1
Modified residuei428PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

PaxDbiF4IW47
PRIDEiF4IW47

PTM databases

iPTMnetiF4IW47

Expressioni

Inductioni

Up-regulated by salt, sorbitol, and abscisic acid (ABA).1 Publication

Gene expression databases

ExpressionAtlasiF4IW47 differential
GenevisibleiF4IW47 AT

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4473, 2 interactors
STRINGi3702.AT2G45290.1

Structurei

3D structure databases

ProteinModelPortaliF4IW47
SMRiF4IW47
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the transketolase family.Curated

Keywords - Domaini

Transit peptide

Phylogenomic databases

eggNOGiKOG0523 Eukaryota
COG0021 LUCA
HOGENOMiHOG000225954
InParanoidiF4IW47
KOiK00615
OMAiYALQQTD
OrthoDBiEOG093603UK

Family and domain databases

Gene3Di3.40.50.920, 1 hit
InterProiView protein in InterPro
IPR029061 THDP-binding
IPR009014 Transketo_C/PFOR_II
IPR005475 Transketolase-like_Pyr-bd
IPR005478 Transketolase_bac-like
IPR020826 Transketolase_BS
IPR033248 Transketolase_C
IPR033247 Transketolase_fam
IPR005474 Transketolase_N
PANTHERiPTHR43522 PTHR43522, 1 hit
PfamiView protein in Pfam
PF02779 Transket_pyr, 1 hit
PF02780 Transketolase_C, 1 hit
PF00456 Transketolase_N, 1 hit
SMARTiView protein in SMART
SM00861 Transket_pyr, 1 hit
SUPFAMiSSF52518 SSF52518, 2 hits
SSF52922 SSF52922, 1 hit
TIGRFAMsiTIGR00232 tktlase_bact, 1 hit
PROSITEiView protein in PROSITE
PS00801 TRANSKETOLASE_1, 1 hit
PS00802 TRANSKETOLASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

F4IW47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASTSSLALS QALLTRAISH NGSENCVSIP AFSALKSTSP RTSGTISSRR
60 70 80 90 100
RNASTISHSL RPLVRAAAVE AIVTSSDSSL VDKSVNTIRF LAIDAVEKAK
110 120 130 140 150
SGHPGLPMGC APMSHILYDE VMKYNPKNPY WFNRDRFVLS AGHGCMLQYA
160 170 180 190 200
LLHLAGYDSV REEDLKSFRQ WGSKTPGHPE NFETPGVEAT TGPLGQGIAN
210 220 230 240 250
AVGLALAEKH LAARFNKPDN EIVDHYTYSI LGDGCQMEGI SNEVCSLAGH
260 270 280 290 300
WGLGKLIAFY DDNHISIDGD TDIAFTESVD KRFEALGWHV IWVKNGNNGY
310 320 330 340 350
DEIRAAIREA KAVTDKPTLI KVTTTIGYGS PNKANSYSVH GAALGEKEVE
360 370 380 390 400
ATRNNLGWPY EPFHVPEDVK SHWSRHTPEG AALEADWNAK FAAYEKKYPE
410 420 430 440 450
EAAELKSIIS GELPVGWEKA LPTYTPDSPG DATRNLSQQC LNALAKAVPG
460 470 480 490 500
FLGGSADLAS SNMTMLKAFG NFQKATPEER NLRFGVREHG MGAICNGIAL
510 520 530 540 550
HSPGFIPYCA TFFVFTDYMR AAMRISALSE AGVIYVMTHD SIGLGEDGPT
560 570 580 590 600
HQPIEHLSSF RAMPNIMMFR PADGNETAGA YKIAVTKRKT PSVLALSRQK
610 620 630 640 650
LPQLPGTSIE SVEKGGYTIS DNSTGNKPDV ILIGTGSELE IAAQAAEKLR
660 670 680 690 700
EQGKSVRVVS FVCWELFDEQ SDAYKESVLP SDVSARVSIE AGSTFGWGKI
710 720 730 740
VGGKGKSIGI DTFGASAPAG KLYKEFGITI EAMVEAAKSL I
Length:741
Mass (Da):79,922
Last modified:June 28, 2011 - v1
Checksum:iC712DFDE2C7D63C6
GO

Sequence cautioni

The sequence AAB82634 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL09768 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC002387 Genomic DNA Translation: AAB82634.2 Different initiation.
CP002685 Genomic DNA Translation: AEC10535.1
CP002685 Genomic DNA Translation: ANM62077.1
AY057528 mRNA Translation: AAL09768.1 Different initiation.
PIRiG84888
RefSeqiNP_001324258.1, NM_001337121.1
NP_566041.2, NM_130092.3
UniGeneiAt.12300
At.67348

Genome annotation databases

EnsemblPlantsiAT2G45290.1; AT2G45290.1; AT2G45290
AT2G45290.2; AT2G45290.2; AT2G45290
GeneIDi819137
GrameneiAT2G45290.1; AT2G45290.1; AT2G45290
AT2G45290.2; AT2G45290.2; AT2G45290
KEGGiath:AT2G45290

Similar proteinsi

Entry informationi

Entry nameiTKTC2_ARATH
AccessioniPrimary (citable) accession number: F4IW47
Secondary accession number(s): O22143, Q93ZH6
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: June 28, 2011
Last modified: May 23, 2018
This is version 59 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Arabidopsis thaliana
    Arabidopsis thaliana: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families
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