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P17709 (HXKG_YEAST) Reviewed, UniProtKB/Swiss-Prot

Last modified June 11, 2014. Version 131. 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 namesRecommended name:
Glucokinase-1

EC=2.7.1.2
Alternative name(s):
Glucose kinase 1
Short name=GLK-1
Gene names
Name:GLK1
Synonyms:HOR3
Ordered Locus Names:YCL040W
ORF Names:YCL312, YCL40W
OrganismSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) [Reference proteome]
Taxonomic identifier559292 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Two isoenzymes, hexokinase-1 and hexokinase-2, can phosphorylate keto- and aldohexoses in yeast, whereas a third isoenzyme, GLK, is specific for aldohexoses. All glucose phosphorylating enzymes are involved in glucose uptake.

Catalytic activity

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

Subunit structure

Monomer.

Miscellaneous

Present with 21100 molecules/cell in log phase SD medium.

Sequence similarities

Belongs to the hexokinase family.

Contains 1 hexokinase type-1 domain.

Contains 1 hexokinase type-2 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.6
Chain2 – 500499Glucokinase-1
PRO_0000197603

Regions

Domain14 – 230217Hexokinase type-1
Domain244 – 500257Hexokinase type-2
Nucleotide binding487 – 4926ATP Potential
Region158 – 18427Glucose-binding Potential

Sites

Binding site1101ATP Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.6 Ref.8
Modified residue21Phosphoserine Ref.6
Modified residue4701Phosphoserine Ref.7

Sequences

Sequence LengthMass (Da)Tools
P17709 [UniParc].

Last modified August 1, 1990. Version 1.
Checksum: A7A417041D7A961F

FASTA50055,377
        10         20         30         40         50         60 
MSFDDLHKAT ERAVIQAVDQ ICDDFEVTPE KLDELTAYFI EQMEKGLAPP KEGHTLASDK 

        70         80         90        100        110        120 
GLPMIPAFVT GSPNGTERGV LLAADLGGTN FRICSVNLHG DHTFSMEQMK SKIPDDLLDD 

       130        140        150        160        170        180 
ENVTSDDLFG FLARRTLAFM KKYHPDELAK GKDAKPMKLG FTFSYPVDQT SLNSGTLIRW 

       190        200        210        220        230        240 
TKGFRIADTV GKDVVQLYQE QLSAQGMPMI KVVALTNDTV GTYLSHCYTS DNTDSMTSGE 

       250        260        270        280        290        300 
ISEPVIGCIF GTGTNGCYME EINKITKLPQ ELRDKLIKEG KTHMIINVEW GSFDNELKHL 

       310        320        330        340        350        360 
PTTKYDVVID QKLSTNPGFH LFEKRVSGMF LGEVLRNILV DLHSQGLLLQ QYRSKEQLPR 

       370        380        390        400        410        420 
HLTTPFQLSS EVLSHIEIDD STGLRETELS LLQSLRLPTT PTERVQIQKL VRAISRRSAY 

       430        440        450        460        470        480 
LAAVPLAAIL IKTNALNKRY HGEVEIGCDG SVVEYYPGFR SMLRHALALS PLGAEGERKV 

       490        500 
HLKIAKDGSG VGAALCALVA 

« Hide

References

« Hide 'large scale' references
[1]"Structure of yeast glucokinase, a strongly diverged specific aldo-hexose-phosphorylating isoenzyme."
Albig W., Entian K.-D.
Gene 73:141-152(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"The complete sequence of a 9,543 bp segment on the left arm of chromosome III reveals five open reading frames including glucokinase and the protein disulfide isomerase."
Scherens B., Messenguy F., Gigot D., Dubois E.
Yeast 8:577-586(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"The complete DNA sequence of yeast chromosome III."
Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M. expand/collapse author list , Carcano C., Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., Tzermia M., Urrestarazu L.A., Valle G., Vetter I., van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.
Nature 357:38-46(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 204508 / S288c.
[4]"The reference genome sequence of Saccharomyces cerevisiae: Then and now."
Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R., Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S., Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.
G3 (Bethesda) 4:389-398(2014) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: ATCC 204508 / S288c.
[5]"Global analysis of protein expression in yeast."
Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N., O'Shea E.K., Weissman J.S.
Nature 425:737-741(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
[6]"Quantitative phosphoproteomics applied to the yeast pheromone signaling pathway."
Gruhler A., Olsen J.V., Mohammed S., Mortensen P., Faergeman N.J., Mann M., Jensen O.N.
Mol. Cell. Proteomics 4:310-327(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
Strain: YAL6B.
[7]"A multidimensional chromatography technology for in-depth phosphoproteome analysis."
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.
Mol. Cell. Proteomics 7:1389-1396(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-470, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[8]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M24077 Genomic DNA. Translation: AAA53536.1.
X59720 Genomic DNA. Translation: CAA42376.1.
BK006937 Genomic DNA. Translation: DAA07444.1.
PIRJT0482.
RefSeqNP_009890.1. NM_001178685.1.

3D structure databases

ProteinModelPortalP17709.
SMRP17709. Positions 25-497.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid30943. 29 interactions.
DIPDIP-525N.
IntActP17709. 5 interactions.
MINTMINT-401461.
STRING4932.YCL040W.

Proteomic databases

MaxQBP17709.
PaxDbP17709.
PeptideAtlasP17709.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiYCL040W; YCL040W; YCL040W.
GeneID850317.
KEGGsce:YCL040W.

Organism-specific databases

CYGDYCL040w.
SGDS000000545. GLK1.

Phylogenomic databases

eggNOGCOG5026.
GeneTreeENSGT00390000017159.
HOGENOMHOG000162670.
KOK00844.
OMAGEVEIGC.
OrthoDBEOG79SF68.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-5982.
YEAST:YCL040W-MONOMER.
SABIO-RKP17709.

Gene expression databases

GenevestigatorP17709.

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

NextBio965721.

Entry information

Entry nameHXKG_YEAST
AccessionPrimary (citable) accession number: P17709
Secondary accession number(s): D6VQX5
Entry history
Integrated into UniProtKB/Swiss-Prot: August 1, 1990
Last sequence update: August 1, 1990
Last modified: June 11, 2014
This is version 131 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Yeast chromosome III

Yeast (Saccharomyces cerevisiae) chromosome III: entries and gene names

Yeast

Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD

SIMILARITY comments

Index of protein domains and families