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Protein

Transketolase-2, chloroplastic

Gene

TKL-2

Organism
Arabidopsis thaliana (Mouse-ear cress)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei103 – 1031SubstrateBy similarity
Sitei103 – 1031Important for catalytic activityBy similarity
Binding sitei143 – 1431Thiamine pyrophosphateBy similarity
Metal bindingi233 – 2331MagnesiumBy similarity
Binding sitei234 – 2341Thiamine pyrophosphate; via amide nitrogenBy similarity
Metal bindingi263 – 2631MagnesiumBy similarity
Binding sitei263 – 2631Thiamine pyrophosphateBy similarity
Metal bindingi265 – 2651Magnesium; via carbonyl oxygenBy similarity
Binding sitei340 – 3401SubstrateBy similarity
Binding sitei340 – 3401Thiamine pyrophosphateBy similarity
Sitei340 – 3401Important for catalytic activityBy similarity
Binding sitei434 – 4341SubstrateBy similarity
Binding sitei461 – 4611SubstrateBy similarity
Active sitei488 – 4881Proton donorBy similarity
Binding sitei488 – 4881Thiamine pyrophosphateBy similarity
Binding sitei515 – 5151Thiamine pyrophosphateBy similarity
Binding sitei539 – 5391SubstrateBy similarity
Binding sitei547 – 5471SubstrateBy similarity
Binding sitei598 – 5981SubstrateBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi192 – 1943Thiamine pyrophosphateBy similarity

GO - Molecular functioni

GO - Biological processi

  • reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
  • response to cadmium ion Source: TAIR
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Ligandi

Calcium, Magnesium, Metal-binding, Thiamine pyrophosphate

Enzyme and pathway databases

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

TAIRiAT2G45290.

Subcellular locationi

GO - Cellular componenti

  • chloroplast Source: TAIR
  • chloroplast stroma Source: TAIR
  • chloroplast thylakoid membrane Source: UniProtKB-SubCell
  • plastid Source: TAIR
Complete GO annotation...

Keywords - Cellular componenti

Chloroplast, Membrane, Plastid, Thylakoid

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Transit peptidei1 – 6565ChloroplastSequence analysisCombined sourcesAdd
BLAST
Chaini66 – 741676Transketolase-2, chloroplasticPRO_0000421818Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei66 – 661N-acetylalanineCombined sources
Modified residuei428 – 4281PhosphoserineBy similarity

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

GenevisibleiF4IW47. AT.

Interactioni

Subunit structurei

Homodimer.By similarity

Protein-protein interaction databases

BioGridi4473. 2 interactions.
STRINGi3702.AT2G45290.1.

Structurei

3D structure databases

ProteinModelPortaliF4IW47.
SMRiF4IW47. Positions 75-740.
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.
OMAiLNWNHGP.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. 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.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]

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 AAB82634.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL09768.1 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.
AY057528 mRNA. Translation: AAL09768.1. Different initiation.
PIRiG84888.
RefSeqiNP_566041.2. NM_130092.2.
UniGeneiAt.12300.
At.67348.

Genome annotation databases

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

Cross-referencesi

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.
AY057528 mRNA. Translation: AAL09768.1. Different initiation.
PIRiG84888.
RefSeqiNP_566041.2. NM_130092.2.
UniGeneiAt.12300.
At.67348.

3D structure databases

ProteinModelPortaliF4IW47.
SMRiF4IW47. Positions 75-740.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4473. 2 interactions.
STRINGi3702.AT2G45290.1.

PTM databases

iPTMnetiF4IW47.

Proteomic databases

PaxDbiF4IW47.
PRIDEiF4IW47.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

TAIRiAT2G45290.

Phylogenomic databases

eggNOGiKOG0523. Eukaryota.
COG0021. LUCA.
HOGENOMiHOG000225954.
InParanoidiF4IW47.
KOiK00615.
OMAiLNWNHGP.

Enzyme and pathway databases

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

Miscellaneous databases

PROiF4IW47.

Gene expression databases

GenevisibleiF4IW47. AT.

Family and domain databases

Gene3Di3.40.50.920. 1 hit.
3.40.50.970. 2 hits.
InterProiIPR029061. 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.
[Graphical view]
PANTHERiPTHR11624. PTHR11624. 2 hits.
PfamiPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTiSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMiSSF52518. SSF52518. 2 hits.
SSF52922. SSF52922. 1 hit.
TIGRFAMsiTIGR00232. tktlase_bact. 1 hit.
PROSITEiPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: cv. Columbia.
  2. The Arabidopsis Information Resource (TAIR)
    Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases
    Cited for: GENOME REANNOTATION.
    Strain: cv. Columbia.
  3. "Empirical analysis of transcriptional activity in the Arabidopsis genome."
    Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M., Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G., Liu S.X., Lam B., Sakano H., Wu T., Yu G.
    , Miranda M., Quach H.L., Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C., Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J., Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A., Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C., Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X., Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M., Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K., Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A., Ecker J.R.
    Science 302:842-846(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 54-741.
    Strain: cv. Columbia.
  4. "The Arabidopsis thaliana chloroplast proteome reveals pathway abundance and novel protein functions."
    Kleffmann T., Russenberger D., von Zychlinski A., Christopher W., Sjoelander K., Gruissem W., Baginsky S.
    Curr. Biol. 14:354-362(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  5. "Sorting signals, N-terminal modifications and abundance of the chloroplast proteome."
    Zybailov B., Rutschow H., Friso G., Rudella A., Emanuelsson O., Sun Q., van Wijk K.J.
    PLoS ONE 3:E1994-E1994(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  6. "The upregulation of thiamine (vitamin B1) biosynthesis in Arabidopsis thaliana seedlings under salt and osmotic stress conditions is mediated by abscisic acid at the early stages of this stress response."
    Rapala-Kozik M., Wolak N., Kujda M., Banas A.K.
    BMC Plant Biol. 12:2-2(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION, FUNCTION.
  7. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-66, CLEAVAGE OF TRANSIT PEPTIDE [LARGE SCALE ANALYSIS] AFTER ARG-65, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiTKTC2_ARATH
AccessioniPrimary (citable) accession number: F4IW47
Secondary accession number(s): O22143, Q93ZH6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 6, 2013
Last sequence update: June 28, 2011
Last modified: May 11, 2016
This is version 45 of the entry and version 1 of the sequence. [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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.