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Protein

Hexokinase

Gene

RAG5

Organism
Kluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

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

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei111 – 1111ATPBy similarity

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. hexokinase activity Source: UniProtKB-EC

GO - Biological processi

  1. glycolytic process Source: UniProtKB-KW
  2. hexose metabolic process Source: UniProtKB-UniPathway
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Glycolysis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.1.1. 2825.
SABIO-RKP33284.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexokinase (EC:2.7.1.1)
Gene namesi
Name:RAG5
Ordered Locus Names:KLLA0D11352g
OrganismiKluyveromyces lactis (strain ATCC 8585 / CBS 2359 / DSM 70799 / NBRC 1267 / NRRL Y-1140 / WM37) (Yeast) (Candida sphaerica)
Taxonomic identifieri284590 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeKluyveromyces
ProteomesiUP000000598 Componenti: Chromosome D

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 485484HexokinasePRO_0000197608Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei15 – 151Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Interactioni

Subunit structurei

Monomer and homodimer. The monomeric form is active, the homodimeric form inactive.1 Publication

Protein-protein interaction databases

STRINGi28985.P33284.

Structurei

Secondary structure

1
485
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi21 – 3414Combined sources
Helixi38 – 5619Combined sources
Beta strandi57 – 593Combined sources
Beta strandi61 – 633Combined sources
Beta strandi79 – 10325Combined sources
Beta strandi105 – 1139Combined sources
Helixi118 – 1203Combined sources
Helixi123 – 14119Combined sources
Beta strandi150 – 1567Combined sources
Beta strandi158 – 1614Combined sources
Beta strandi163 – 1664Combined sources
Helixi187 – 19711Combined sources
Beta strandi202 – 2087Combined sources
Helixi210 – 22112Combined sources
Beta strandi225 – 24218Combined sources
Helixi243 – 2453Combined sources
Helixi247 – 2493Combined sources
Turni250 – 2523Combined sources
Beta strandi262 – 2665Combined sources
Helixi269 – 2713Combined sources
Turni272 – 2754Combined sources
Beta strandi277 – 2793Combined sources
Helixi283 – 2919Combined sources
Beta strandi292 – 2943Combined sources
Helixi299 – 3046Combined sources
Turni306 – 3083Combined sources
Helixi309 – 32214Combined sources
Beta strandi325 – 3273Combined sources
Helixi333 – 3364Combined sources
Helixi344 – 3518Combined sources
Helixi358 – 36811Combined sources
Helixi374 – 40633Combined sources
Beta strandi409 – 4179Combined sources
Helixi418 – 4225Combined sources
Helixi426 – 43813Combined sources
Helixi445 – 4473Combined sources
Beta strandi449 – 4546Combined sources
Turni458 – 4603Combined sources
Helixi461 – 47616Combined sources
Beta strandi480 – 4823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP33284.
SMRiP33284. Positions 18-484.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP33284.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini21 – 468448HexokinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni75 – 208134Hexokinase small subdomainPROSITE-ProRule annotationAdd
BLAST
Regioni151 – 17727Glucose-bindingSequence AnalysisAdd
BLAST
Regioni209 – 457249Hexokinase large subdomainPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the hexokinase family.PROSITE-ProRule annotationCurated
Contains 1 hexokinase domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG5026.
HOGENOMiHOG000162670.
InParanoidiP33284.
KOiK00844.
OMAiEELWSFI.
OrthoDBiEOG79SF68.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
PROSITEiPS00378. HEXOKINASE_1. 1 hit.
PS51748. HEXOKINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P33284-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MVRLGPKKPP ARKGSMADVP ANLMEQIHGL ETLFTVSSEK MRSIVKHFIS
60 70 80 90 100
ELDKGLSKKG GNIPMIPGWV VEYPTGKETG DFLALDLGGT NLRVVLVKLG
110 120 130 140 150
GNHDFDTTQN KYRLPDHLRT GTSEQLWSFI AKCLKEFVDE WYPDGVSEPL
160 170 180 190 200
PLGFTFSYPA SQKKINSGVL QRWTKGFDIE GVEGHDVVPM LQEQIEKLNI
210 220 230 240 250
PINVVALIND TTGTLVASLY TDPQTKMGII IGTGVNGAYY DVVSGIEKLE
260 270 280 290 300
GLLPEDIGPD SPMAINCEYG SFDNEHLVLP RTKYDVIIDE ESPRPGQQAF
310 320 330 340 350
EKMTSGYYLG EIMRLVLLDL YDSGFIFKDQ DISKLKEAYV MDTSYPSKIE
360 370 380 390 400
DDPFENLEDT DDLFKTNLNI ETTVVERKLI RKLAELVGTR AARLTVCGVS
410 420 430 440 450
AICDKRGYKT AHIAADGSVF NRYPGYKEKA AQALKDIYNW DVEKMEDHPI
460 470 480
QLVAAEDGSG VGAAIIACLT QKRLAAGKSV GIKGE
Length:485
Mass (Da):53,610
Last modified:January 22, 2007 - v3
Checksum:i3E93D80C92663FB0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti206 – 2061A → R in CAA43855 (PubMed:8321195).Curated

Mass spectrometryi

Molecular mass is 53476±5 Da from positions 2 - 485. Determined by ESI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61680 Genomic DNA. Translation: CAA43855.1.
CR382124 Genomic DNA. Translation: CAH00663.1.
PIRiA48132.
RefSeqiXP_453567.1. XM_453567.1.

Genome annotation databases

GeneIDi2893280.
KEGGikla:KLLA0D11352g.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X61680 Genomic DNA. Translation: CAA43855.1.
CR382124 Genomic DNA. Translation: CAH00663.1.
PIRiA48132.
RefSeqiXP_453567.1. XM_453567.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP33284.
SMRiP33284. Positions 18-484.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi28985.P33284.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi2893280.
KEGGikla:KLLA0D11352g.

Phylogenomic databases

eggNOGiCOG5026.
HOGENOMiHOG000162670.
InParanoidiP33284.
KOiK00844.
OMAiEELWSFI.
OrthoDBiEOG79SF68.

Enzyme and pathway databases

UniPathwayiUPA00242.
BRENDAi2.7.1.1. 2825.
SABIO-RKP33284.

Miscellaneous databases

EvolutionaryTraceiP33284.

Family and domain databases

InterProiIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERiPTHR19443. PTHR19443. 1 hit.
PfamiPF00349. Hexokinase_1. 1 hit.
PF03727. Hexokinase_2. 1 hit.
[Graphical view]
PRINTSiPR00475. HEXOKINASE.
PROSITEiPS00378. HEXOKINASE_1. 1 hit.
PS51748. HEXOKINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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(1992) [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.
    , 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(2003) [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(2002) [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.

Entry informationi

Entry nameiHXK_KLULA
AccessioniPrimary (citable) accession number: P33284
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 31, 1994
Last sequence update: January 22, 2007
Last modified: March 31, 2015
This is version 111 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.