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Protein

Hexokinase-2

Gene

hxk2

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript leveli

Functioni

Catalytic activityi

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

Pathwayi: hexose metabolism

This protein is involved in the pathway hexose metabolism, which is part of Carbohydrate metabolism.
View all proteins of this organism that are known to be involved in the pathway hexose metabolism and in Carbohydrate metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei93 – 931ATPBy similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • fructokinase activity Source: PomBase
  • glucokinase activity Source: PomBase
  • glucose binding Source: InterPro
  • mannokinase activity Source: PomBase

GO - Biological processi

  • canonical glycolysis Source: PomBase
  • cellular glucose homeostasis Source: InterPro
  • fructose 6-phosphate metabolic process Source: PomBase
  • glucose 6-phosphate metabolic process Source: PomBase
  • glycolytic fermentation Source: PomBase
  • mannose metabolic process Source: PomBase
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. 5613.
ReactomeiR-SPO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-SPO-70153. Glucose transport.
R-SPO-70171. Glycolysis.
SABIO-RKP50521.
UniPathwayiUPA00242.

Names & Taxonomyi

Protein namesi
Recommended name:
Hexokinase-2 (EC:2.7.1.1)
Gene namesi
Name:hxk2
ORF Names:SPAC4F8.07c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
Proteomesi
  • UP000002485 Componenti: Chromosome I

Organism-specific databases

EuPathDBiFungiDB:SPAC4F8.07c.
PomBaseiSPAC4F8.07c. hxk2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: PomBase
  • nucleus Source: PomBase
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 455455Hexokinase-2PRO_0000197610Add
BLAST

Proteomic databases

MaxQBiP50521.

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi280022. 6 interactions.
MINTiMINT-4690647.

Structurei

3D structure databases

ProteinModelPortaliP50521.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 445443HexokinasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni57 – 195139Hexokinase small subdomainPROSITE-ProRule annotationAdd
BLAST
Regioni138 – 16427Glucose-bindingSequence analysisAdd
BLAST
Regioni196 – 434239Hexokinase large subdomainPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

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

Phylogenomic databases

HOGENOMiHOG000162670.
InParanoidiP50521.
KOiK00844.
OMAiAYVEDIT.
OrthoDBiEOG79SF68.
PhylomeDBiP50521.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

P50521-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEANFQQAVK KLVNDFEYPT ESLREAVKEF DELRQKGLQK NGEVLAMAPA
60 70 80 90 100
FISTLPTGAE TGDFLALDFG GTNLRVCWIQ LLGDGKYEMK HSKSVLPREC
110 120 130 140 150
VRNESVKPII DFMSDHVELF IKEHFPSKFG CPEEEYLPMG FTFSYPANQV
160 170 180 190 200
SITESYLLRW TKGLNIPEAI NKDFAQFLTE GFKARNLPIR IEAVINDTVG
210 220 230 240 250
TLVTRAYTSK ESDTFMGIIF GTGTNGAYVE QMNQIPKLAG KCTGDHMLIN
260 270 280 290 300
MEWGATDFSC LHSTRYDLLL DHDTPNAGRQ IFEKRVGGMY LGELFRRALF
310 320 330 340 350
HLIKVYNFNE GIFPPSITDA WSLETSVLSR MMVERSAENV RNVLSTFKFR
360 370 380 390 400
FRSDEEALYL WDAAHAIGRR AARMSAVPIA SLYLSTGRAG KKSDVGVDGS
410 420 430 440 450
LVEHYPHFVD MLREALRELI GDNEKLISIG IAKDGSGIGA ALCALQAVKE

KKGLA
Length:455
Mass (Da):50,920
Last modified:October 1, 1996 - v1
Checksum:i9751F9969F63AC96
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti295 – 2951F → S in BAA13859 (PubMed:9501991).Curated
Sequence conflicti298 – 2981A → V in BAA13859 (PubMed:9501991).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92895 mRNA. Translation: CAA63488.1.
CU329670 Genomic DNA. Translation: CAB11054.1.
D89198 mRNA. Translation: BAA13859.1.
PIRiS68693.
T42997.
RefSeqiNP_593865.1. NM_001019294.2.

Genome annotation databases

EnsemblFungiiSPAC4F8.07c.1; SPAC4F8.07c.1:pep; SPAC4F8.07c.
GeneIDi2543607.
KEGGispo:SPAC4F8.07c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X92895 mRNA. Translation: CAA63488.1.
CU329670 Genomic DNA. Translation: CAB11054.1.
D89198 mRNA. Translation: BAA13859.1.
PIRiS68693.
T42997.
RefSeqiNP_593865.1. NM_001019294.2.

3D structure databases

ProteinModelPortaliP50521.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi280022. 6 interactions.
MINTiMINT-4690647.

Proteomic databases

MaxQBiP50521.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPAC4F8.07c.1; SPAC4F8.07c.1:pep; SPAC4F8.07c.
GeneIDi2543607.
KEGGispo:SPAC4F8.07c.

Organism-specific databases

EuPathDBiFungiDB:SPAC4F8.07c.
PomBaseiSPAC4F8.07c. hxk2.

Phylogenomic databases

HOGENOMiHOG000162670.
InParanoidiP50521.
KOiK00844.
OMAiAYVEDIT.
OrthoDBiEOG79SF68.
PhylomeDBiP50521.

Enzyme and pathway databases

UniPathwayiUPA00242.
BRENDAi2.7.1.1. 5613.
ReactomeiR-SPO-170822. Regulation of Glucokinase by Glucokinase Regulatory Protein.
R-SPO-70153. Glucose transport.
R-SPO-70171. Glycolysis.
SABIO-RKP50521.

Miscellaneous databases

NextBioi20804614.
PROiP50521.

Family and domain databases

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

Publicationsi

« Hide 'large scale' publications
  1. "Schizosaccharomyces pombe possesses an unusual and a conventional hexokinase: biochemical and molecular characterization of both hexokinases."
    Petit T., Blazquez M.A., Gancedo C.
    FEBS Lett. 378:185-189(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The genome sequence of Schizosaccharomyces pombe."
    Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.
    , Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "Identification of open reading frames in Schizosaccharomyces pombe cDNAs."
    Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.
    DNA Res. 4:363-369(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 20-455.
    Strain: PR745.

Entry informationi

Entry nameiHXK2_SCHPO
AccessioniPrimary (citable) accession number: P50521
Secondary accession number(s): P78848
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.