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P33284 (HXK_KLULA) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 104. 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

Names and origin

Protein attributes

Sequence length485 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + D-hexose = ADP + D-hexose 6-phosphate.

Pathway

Carbohydrate metabolism; hexose metabolism.

Subunit structure

Monomer and homodimer. The monomeric form is active, the homodimeric form inactive. Ref.3

Sequence similarities

Belongs to the hexokinase family.

Contains 1 hexokinase type-1 domain.

Contains 1 hexokinase type-2 domain.

Mass spectrometry

Molecular mass is 53476±5 Da from positions 2 - 485. Determined by ESI. Ref.3

Ontologies

Keywords
   Biological processGlycolysis
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMPhosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

hexokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 485484Hexokinase
PRO_0000197608

Regions

Domain22 – 222201Hexokinase type-1
Domain224 – 472249Hexokinase type-2
Region151 – 17727Glucose-binding Potential

Sites

Binding site1111ATP By similarity

Amino acid modifications

Modified residue151Phosphoserine Ref.3

Experimental info

Sequence conflict2061A → R in CAA43855. Ref.1

Secondary structure

......................................................................... 485
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P33284 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 3E93D80C92663FB0

FASTA48553,610
        10         20         30         40         50         60 
MVRLGPKKPP ARKGSMADVP ANLMEQIHGL ETLFTVSSEK MRSIVKHFIS ELDKGLSKKG 

        70         80         90        100        110        120 
GNIPMIPGWV VEYPTGKETG DFLALDLGGT NLRVVLVKLG GNHDFDTTQN KYRLPDHLRT 

       130        140        150        160        170        180 
GTSEQLWSFI AKCLKEFVDE WYPDGVSEPL PLGFTFSYPA SQKKINSGVL QRWTKGFDIE 

       190        200        210        220        230        240 
GVEGHDVVPM LQEQIEKLNI PINVVALIND TTGTLVASLY TDPQTKMGII IGTGVNGAYY 

       250        260        270        280        290        300 
DVVSGIEKLE GLLPEDIGPD SPMAINCEYG SFDNEHLVLP RTKYDVIIDE ESPRPGQQAF 

       310        320        330        340        350        360 
EKMTSGYYLG EIMRLVLLDL YDSGFIFKDQ DISKLKEAYV MDTSYPSKIE DDPFENLEDT 

       370        380        390        400        410        420 
DDLFKTNLNI ETTVVERKLI RKLAELVGTR AARLTVCGVS AICDKRGYKT AHIAADGSVF 

       430        440        450        460        470        480 
NRYPGYKEKA AQALKDIYNW DVEKMEDHPI QLVAAEDGSG VGAAIIACLT QKRLAAGKSV 


GIKGE 

« Hide

References

« Hide 'large scale' references
[1]"The hexokinase gene is required for transcriptional regulation of the glucose transporter gene RAG1 in Kluyveromyces lactis."
Prior C., Mamessier P., Fukuhara H., Chen X.J., Wesolowski-Louvel M.
Mol. Cell. Biol. 13:3882-3889(1993) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 76492 / CBS 2359/152 / CLIB 210 and PM6-7A.
[2]"Genome evolution in yeasts."
Dujon B., Sherman D., Fischer G., Durrens P., Casaregola S., Lafontaine I., de Montigny J., Marck C., Neuveglise C., Talla E., Goffard N., Frangeul L., Aigle M., Anthouard V., Babour A., Barbe V., Barnay S., Blanchin S. expand/collapse author list , Beckerich J.-M., Beyne E., Bleykasten C., Boisrame A., Boyer J., Cattolico L., Confanioleri F., de Daruvar A., Despons L., Fabre E., Fairhead C., Ferry-Dumazet H., Groppi A., Hantraye F., Hennequin C., Jauniaux N., Joyet P., Kachouri R., Kerrest A., Koszul R., Lemaire M., Lesur I., Ma L., Muller H., Nicaud J.-M., Nikolski M., Oztas S., Ozier-Kalogeropoulos O., Pellenz S., Potier S., Richard G.-F., Straub M.-L., Suleau A., Swennen D., Tekaia F., Wesolowski-Louvel M., Westhof E., Wirth B., Zeniou-Meyer M., Zivanovic Y., Bolotin-Fukuhara M., Thierry A., Bouchier C., Caudron B., Scarpelli C., Gaillardin C., Weissenbach J., Wincker P., Souciet J.-L.
Nature 430:35-44(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37.
[3]"The unique hexokinase of Kluyveromyces lactis. Molecular and functional characterization and evaluation of a role in glucose signaling."
Baer D., Golbik R., Huebner G., Lilie H., Mueller E.-C., Naumann M., Otto A., Reuter R., Breunig K.D., Kriegel T.M.
J. Biol. Chem. 278:39280-39286(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-21; 136-163 AND 198-226, MASS SPECTROMETRY, SUBUNIT, PHOSPHORYLATION AT SER-15.
Strain: ATCC 76492 / CBS 2359/152 / CLIB 210.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X61680 Genomic DNA. Translation: CAA43855.1.
CR382124 Genomic DNA. Translation: CAH00663.1.
PIRA48132.
RefSeqXP_453567.1. XM_453567.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3O08X-ray2.00A/B1-485[»]
3O1BX-ray2.80A1-485[»]
3O1WX-ray1.66A/B1-485[»]
3O4WX-ray1.61A/B1-485[»]
3O5BX-ray1.97A/B1-485[»]
3O6WX-ray1.48A/B1-485[»]
3O80X-ray2.18A1-485[»]
3O8MX-ray1.42A1-485[»]
4JAXX-ray2.26A/B/C/D/E/F1-485[»]
ProteinModelPortalP33284.
SMRP33284. Positions 18-484.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING28985.P33284.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2893280.
KEGGkla:KLLA0D11352g.

Phylogenomic databases

eggNOGCOG5026.
HOGENOMHOG000162670.
KOK00844.
OMAFDIPNVE.
OrthoDBEOG79SF68.

Enzyme and pathway databases

BRENDA2.7.1.1. 2825.
SABIO-RKP33284.
UniPathwayUPA00242.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERPTHR19443. PTHR19443. 1 hit.
PfamPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP33284.

Entry information

Entry nameHXK_KLULA
AccessionPrimary (citable) accession number: P33284
Entry history
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 104 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways