Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7SIC9 (TKTC_MAIZE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 16, 2011. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Transketolase, chloroplastic
Short name=TK
EC=2.2.1.1
OrganismZea mays (Maize)
Taxonomic identifier4577 [NCBI]
Taxonomic lineageEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliophyta › Liliopsida › Poales › Poaceae › PACMAD clade › Panicoideae › Andropogoneae › Zea

Protein attributes

Sequence length675 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1

Catalytic activity

Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. Ref.1

Cofactor

Binds 1 magnesium ion per subunit. Ref.1

Binds 1 thiamine pyrophosphate per subunit. Ref.1

Pathway

Carbohydrate biosynthesis; Calvin cycle.

Subunit structure

Homodimer. Ref.1

Subcellular location

Plastid › chloroplast thylakoid membrane By similarity.

Sequence similarities

Belongs to the transketolase family. Ref.1

Biophysicochemical properties

Kinetic parameters:

KM=581 µM for ribulose-5-phosphate Ref.1

KM=403 µM for xyulose-5-phosphate Ref.1

Vmax=25.3 µmol/min/mg enzyme with ribulose-5-phosphate as substrate Ref.1

Mass spectrometry

Molecular mass is 72994.8 Da from positions 1 - 675. Determined by ESI. Ref.1

Sequence caution

The sequence AAN65341.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentChloroplast
Membrane
Plastid
Thylakoid
   LigandMagnesium
Metal-binding
Thiamine pyrophosphate
   Molecular functionTransferase
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Cellular componentchloroplast thylakoid membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionmetal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

transketolase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 675675Transketolase, chloroplastic
PRO_0000232420

Regions

Nucleotide binding127 – 1293Thiamine pyrophosphate Ref.1
Nucleotide binding168 – 1692Thiamine pyrophosphate Ref.1
Nucleotide binding198 – 2025Thiamine pyrophosphate Ref.1
Nucleotide binding450 – 4534Thiamine pyrophosphate; in homodimeric partner Ref.1

Sites

Metal binding1681Magnesium Ref.1
Metal binding1981Magnesium Ref.1
Metal binding2001Magnesium; via carbonyl oxygen Ref.1
Binding site781Thiamine pyrophosphate Ref.1
Binding site1731Thiamine pyrophosphate Ref.1
Binding site2751Thiamine pyrophosphate Ref.1
Binding site4231Thiamine pyrophosphate; in homodimeric partner Ref.1

Secondary structure

1 ........................................................................................................... 675
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7SIC9 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 3F356BC2D0396510

FASTA67572,993
        10         20         30         40         50         60 
GAVETLQGKA ATGELLEKSV NTIRFLAIDA VEKANSGHPG LPMGCAPMGH VLYDEVMRYN 

        70         80         90        100        110        120 
PKNPYWFNRD RFVLSAGHGC MLQYALLHLA GYDSVKEEDL KQFRQWGSRT PGHPENFETP 

       130        140        150        160        170        180 
GVEVTTGPLG QGIANAVGLA LAEKHLAARF NKPDSEIVDH YTYVILGDGC QMEGIANEAC 

       190        200        210        220        230        240 
SLAGHWGLGK LIAFYDDNHI SIDGDTEIAF TEDVSTRFEA LGWHTIWVKN GNTGYDDIRA 

       250        260        270        280        290        300 
AIKEAKAVTD KPTLIKVTTT IGFGSPNKAN SYSVHGSALG AKEVEATRQN LGWPYDTFFV 

       310        320        330        340        350        360 
PEDVKSHWSR HTPEGAALEA DWNAKFAEYE KKYADDAATL KSIITGELPT GWVDALPKYT 

       370        380        390        400        410        420 
PESPGDATRN LSQQCLNALA NVVPGLIGGS ADLASSNMTL LKMFGDFQKD TAEERNVRFG 

       430        440        450        460        470        480 
VREHGMGAIC NGIALHSPGF VPYCATFFVF TDYMRGAMRI SALSEAGVIY VMTHDSIGLG 

       490        500        510        520        530        540 
EDGPTHQPIE HLVSFRAMPN ILMLRPADGN ETAGAYKVAV LNRKRPSILA LSRQKLPHLP 

       550        560        570        580        590        600 
GTSIEGVEKG GYTISDNSTG NKPDLIVMGT GSELEIAAKA ADELRKEGKT VRVVSFVSWE 

       610        620        630        640        650        660 
LFDEQSDEYK ESVLPAAVTA RISIEAGSTL GWQKYVGAQG KAIGIDKFGA SAPAGTIYKE 

       670 
YGITVESIIA AAKSF

« Hide

References

[1]"Structure and properties of an engineered transketolase from maize."
Gerhardt S., Echt S., Busch M., Freigang J., Auerbach G., Bader G., Martin W.F., Bacher A., Huber R., Fischer M.
Plant Physiol. 132:1941-1949(2003) [PubMed: 12913150] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 1-10, X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEX WITH COFACTOR, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, MASS SPECTROMETRY.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY148193 Other DNA. Translation: AAN65341.1. Different initiation.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ITZX-ray2.30A/B/C1-675[»]
ProteinModelPortalQ7SIC9.
SMRQ7SIC9. Positions 10-675.
ModBaseSearch...

Proteomic databases

PRIDEQ7SIC9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Organism-specific databases

GrameneQ7SIC9.
MaizeGDB320183.

Phylogenomic databases

GeneTreeEPGT00070000029231.

Family and domain databases

InterProIPR009014. Transketo_C/Pyr-ferredox_oxred.
IPR015941. Transketolase-like_C.
IPR005475. Transketolase-like_Pyr-bd.
IPR005478. Transketolase_bac-like.
IPR005476. Transketolase_C.
IPR005474. Transketolase_N.
[Graphical view]
Gene3DG3DSA:3.40.50.920. Transketo_C_like. 1 hit.
PfamPF02779. Transket_pyr. 1 hit.
PF02780. Transketolase_C. 1 hit.
PF00456. Transketolase_N. 1 hit.
[Graphical view]
SMARTSM00861. Transket_pyr. 1 hit.
[Graphical view]
SUPFAMSSF52922. Transketo_C_like. 1 hit.
TIGRFAMsTIGR00232. Tktlase_bact. 1 hit.
PROSITEPS00801. TRANSKETOLASE_1. 1 hit.
PS00802. TRANSKETOLASE_2. False negative.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameTKTC_MAIZE
AccessionPrimary (citable) accession number: Q7SIC9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 18, 2006
Last sequence update: December 15, 2003
Last modified: November 16, 2011
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

Relevant documents

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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents