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UniProtKB - Q7SIC9 (TKTC_MAIZE)
Protein
Transketolase, chloroplastic
Gene
N/A
Organism
Zea mays (Maize)
Status
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.
1 PublicationCatalytic activityi
- D-glyceraldehyde 3-phosphate + D-sedoheptulose 7-phosphate = aldehydo-D-ribose 5-phosphate + D-xylulose 5-phosphate1 PublicationEC:2.2.1.11 Publication
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 diphosphate1 PublicationNote: Binds 1 thiamine pyrophosphate per subunit.1 Publication
Kineticsi
- KM=581 µM for ribulose-5-phosphate1 Publication
- KM=403 µM for xyulose-5-phosphate1 Publication
- Vmax=25.3 µmol/min/mg enzyme with ribulose-5-phosphate as substrate1 Publication
: Calvin cycle Pathwayi
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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Sitei | 38 | Important for catalytic activityBy similarity | 1 | |
Binding sitei | 78 | Thiamine pyrophosphate1 Publication | 1 | |
Metal bindingi | 168 | Magnesium1 Publication | 1 | |
Binding sitei | 169 | Thiamine pyrophosphate; via amide nitrogenBy similarity | 1 | |
Binding sitei | 173 | Thiamine pyrophosphate1 Publication | 1 | |
Metal bindingi | 198 | Magnesium1 Publication | 1 | |
Binding sitei | 198 | Thiamine pyrophosphateBy similarity | 1 | |
Metal bindingi | 200 | Magnesium; via carbonyl oxygen | 1 | |
Binding sitei | 275 | SubstrateBy similarity | 1 | |
Binding sitei | 275 | Thiamine pyrophosphate1 Publication | 1 | |
Sitei | 275 | Important for catalytic activityBy similarity | 1 | |
Binding sitei | 369 | SubstrateBy similarity | 1 | |
Binding sitei | 396 | SubstrateBy similarity | 1 | |
Active sitei | 423 | Proton donorBy similarity | 1 | |
Binding sitei | 423 | Thiamine pyrophosphate; in homodimeric partner1 Publication | 1 | |
Binding sitei | 474 | SubstrateBy similarity | 1 | |
Binding sitei | 482 | SubstrateBy similarity | 1 | |
Binding sitei | 533 | SubstrateBy similarity | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 127 – 129 | Thiamine pyrophosphate1 Publication | 3 | |
Nucleotide bindingi | 450 – 453 | Thiamine pyrophosphate; in homodimeric partner1 Publication | 4 |
GO - Molecular functioni
- calcium ion binding Source: AgBase
- cobalt ion binding Source: AgBase
- manganese ion binding Source: AgBase
- transketolase activity Source: AgBase
GO - Biological processi
- pentose-phosphate shunt Source: GO_Central
- reductive pentose-phosphate cycle Source: UniProtKB-UniPathway
Keywordsi
Molecular function | Transferase |
Ligand | Magnesium, Metal-binding, Thiamine pyrophosphate |
Enzyme and pathway databases
SABIO-RKi | Q7SIC9 |
UniPathwayi | UPA00116 |
Names & Taxonomyi
Protein namesi | |
Organismi | Zea mays (Maize) |
Taxonomic identifieri | 4577 [NCBI] |
Taxonomic lineagei | Eukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogonodae › Andropogoneae › Tripsacinae › Zea |
Proteomesi |
|
Organism-specific databases
MaizeGDBi | 320183 |
Subcellular locationi
Chloroplast
- chloroplast thylakoid membrane By similarity
Chloroplast
- chloroplast thylakoid membrane Source: UniProtKB-SubCell
Cytosol
- cytosol Source: GO_Central
Keywords - Cellular componenti
Chloroplast, Membrane, Plastid, ThylakoidPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000232420 | 1 – 675 | Transketolase, chloroplasticAdd BLAST | 675 |
Proteomic databases
PaxDbi | Q7SIC9 |
PRIDEi | Q7SIC9 |
Interactioni
Subunit structurei
Homodimer.
1 PublicationProtein-protein interaction databases
STRINGi | 4577.GRMZM2G033208_P01 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
SMRi | Q7SIC9 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | Q7SIC9 |
Family & Domainsi
Sequence similaritiesi
Belongs to the transketolase family.1 Publication
Phylogenomic databases
eggNOGi | KOG0523, Eukaryota |
Family and domain databases
CDDi | cd02012, TPP_TK, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
InterProi | View protein in InterPro IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR005478, Transketolase_bac-like IPR033248, Transketolase_C IPR033247, Transketolase_fam IPR005474, Transketolase_N |
PANTHERi | PTHR43522, PTHR43522, 1 hit |
Pfami | View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00232, tktlase_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit |
i Sequence
Sequence statusi: Complete.
Q7SIC9-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
GAVETLQGKA ATGELLEKSV NTIRFLAIDA VEKANSGHPG LPMGCAPMGH
60 70 80 90 100
VLYDEVMRYN PKNPYWFNRD RFVLSAGHGC MLQYALLHLA GYDSVKEEDL
110 120 130 140 150
KQFRQWGSRT PGHPENFETP GVEVTTGPLG QGIANAVGLA LAEKHLAARF
160 170 180 190 200
NKPDSEIVDH YTYVILGDGC QMEGIANEAC SLAGHWGLGK LIAFYDDNHI
210 220 230 240 250
SIDGDTEIAF TEDVSTRFEA LGWHTIWVKN GNTGYDDIRA AIKEAKAVTD
260 270 280 290 300
KPTLIKVTTT IGFGSPNKAN SYSVHGSALG AKEVEATRQN LGWPYDTFFV
310 320 330 340 350
PEDVKSHWSR HTPEGAALEA DWNAKFAEYE KKYADDAATL KSIITGELPT
360 370 380 390 400
GWVDALPKYT PESPGDATRN LSQQCLNALA NVVPGLIGGS ADLASSNMTL
410 420 430 440 450
LKMFGDFQKD TAEERNVRFG VREHGMGAIC NGIALHSPGF VPYCATFFVF
460 470 480 490 500
TDYMRGAMRI SALSEAGVIY VMTHDSIGLG EDGPTHQPIE HLVSFRAMPN
510 520 530 540 550
ILMLRPADGN ETAGAYKVAV LNRKRPSILA LSRQKLPHLP GTSIEGVEKG
560 570 580 590 600
GYTISDNSTG NKPDLIVMGT GSELEIAAKA ADELRKEGKT VRVVSFVSWE
610 620 630 640 650
LFDEQSDEYK ESVLPAAVTA RISIEAGSTL GWQKYVGAQG KAIGIDKFGA
660 670
SAPAGTIYKE YGITVESIIA AAKSF
Sequence cautioni
The sequence AAN65341 differs from that shown. Reason: Erroneous initiation.Curated
Mass spectrometryi
Molecular mass is 72994.8 Da. Determined by ESI. 1 Publication
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY148193 Other DNA Translation: AAN65341.1 Different initiation. |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | AY148193 Other DNA Translation: AAN65341.1 Different initiation. |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1ITZ | X-ray | 2.30 | A/B/C | 1-675 | [»] | |
SMRi | Q7SIC9 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 4577.GRMZM2G033208_P01 |
Proteomic databases
PaxDbi | Q7SIC9 |
PRIDEi | Q7SIC9 |
Organism-specific databases
MaizeGDBi | 320183 |
Phylogenomic databases
eggNOGi | KOG0523, Eukaryota |
Enzyme and pathway databases
UniPathwayi | UPA00116 |
SABIO-RKi | Q7SIC9 |
Miscellaneous databases
EvolutionaryTracei | Q7SIC9 |
Gene expression databases
ExpressionAtlasi | Q7SIC9, baseline and differential |
Family and domain databases
CDDi | cd02012, TPP_TK, 1 hit |
Gene3Di | 3.40.50.920, 1 hit |
InterProi | View protein in InterPro IPR029061, THDP-binding IPR009014, Transketo_C/PFOR_II IPR005475, Transketolase-like_Pyr-bd IPR005478, Transketolase_bac-like IPR033248, Transketolase_C IPR033247, Transketolase_fam IPR005474, Transketolase_N |
PANTHERi | PTHR43522, PTHR43522, 1 hit |
Pfami | View protein in Pfam PF02779, Transket_pyr, 1 hit PF02780, Transketolase_C, 1 hit PF00456, Transketolase_N, 1 hit |
SMARTi | View protein in SMART SM00861, Transket_pyr, 1 hit |
SUPFAMi | SSF52518, SSF52518, 2 hits SSF52922, SSF52922, 1 hit |
TIGRFAMsi | TIGR00232, tktlase_bact, 1 hit |
PROSITEi | View protein in PROSITE PS00801, TRANSKETOLASE_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | TKTC_MAIZE | |
Accessioni | Q7SIC9Primary (citable) accession number: Q7SIC9 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | April 18, 2006 |
Last sequence update: | December 15, 2003 | |
Last modified: | June 2, 2021 | |
This is version 95 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Plant Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structure, Direct protein sequencing, Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families