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P05708 (HXK1_RAT) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 122. 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:
Hexokinase-1
EC=2.7.1.1
Alternative name(s):
Brain form hexokinase
Hexokinase type I
Short name=HK I
Gene names
Name:Hk1
OrganismRattus norvegicus (Rat) [Reference proteome]
Taxonomic identifier10116 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Rattus

Protein attributes

Sequence length918 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

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

Enzyme regulation

Hexokinase is an allosteric enzyme inhibited by its product Glc-6-P.

Pathway

Carbohydrate metabolism; hexose metabolism.

Subunit structure

Monomer.

Subcellular location

Mitochondrion outer membrane. Note: Its hydrophobic N-terminal sequence may be involved in membrane binding.

Tissue specificity

Expressed in flagella of epididymal sperm. Ref.8

Domain

The N- and C-terminal halves of this hexokinase show extensive sequence similarity to each other. The catalytic activity is associated with the C-terminus while regulatory function is associated with the N-terminus. Each domain can bind a single glucose and Gluc-6-P molecule.

Miscellaneous

In vertebrates there are four major glucose-phosphorylating isoenzymes, designated hexokinase I, II, III and IV (glucokinase).

Sequence similarities

Belongs to the hexokinase family.

Ontologies

Keywords
   Biological processGlycolysis
   Cellular componentMembrane
Mitochondrion
Mitochondrion outer membrane
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from direct assay PubMed 15574336PubMed 4353083PubMed 8255543. Source: RGD

negative regulation of apoptotic process

Inferred from mutant phenotype PubMed 15574336. Source: RGD

peptidyl-serine phosphorylation

Inferred from direct assay PubMed 7531990. Source: RGD

peptidyl-threonine phosphorylation

Inferred from direct assay PubMed 7531990. Source: RGD

peptidyl-tyrosine phosphorylation

Inferred from direct assay PubMed 7531990. Source: RGD

protein autophosphorylation

Inferred from direct assay PubMed 2059200PubMed 7531990. Source: RGD

regulation of anion channel activity

Inferred from direct assay PubMed 14561215. Source: RGD

   Cellular_componentcaveola

Inferred from direct assay PubMed 16419038. Source: RGD

cytosol

Inferred from direct assay PubMed 15562563. Source: RGD

mitochondrial outer membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from direct assay PubMed 15562563PubMed 15574336. Source: RGD

protein complex

Inferred from direct assay PubMed 9459579. Source: RGD

   Molecular_functionATP binding

Inferred from direct assay PubMed 15562563. Source: RGD

ATPase activity

Inferred by curator PubMed 15574336. Source: RGD

glucokinase activity

Inferred from direct assay PubMed 15574336. Source: RGD

glucose binding

Inferred from direct assay PubMed 15562563PubMed 15574336Ref.9. Source: RGD

protein complex binding

Inferred from direct assay PubMed 14561215. Source: RGD

protein homodimerization activity

Inferred from direct assay Ref.9. Source: RGD

protein kinase activity

Inferred from direct assay PubMed 7531990. Source: RGD

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 918918Hexokinase-1
PRO_0000197586

Regions

Nucleotide binding84 – 896ATP 1 Potential
Nucleotide binding425 – 4262ATP 1 By similarity
Nucleotide binding532 – 5376ATP 2 By similarity
Nucleotide binding747 – 7482ATP 2 By similarity
Nucleotide binding784 – 7885ATP 2 By similarity
Nucleotide binding863 – 8675ATP 2 By similarity
Region1 – 1212Hydrophobic
Region13 – 475463Regulatory
Region84 – 885Glucose-6-phosphate 1 binding
Region172 – 1732Substrate 1 binding
Region208 – 2092Substrate 1 binding
Region291 – 2944Substrate 1 binding
Region413 – 4153Glucose-6-phosphate 1 binding
Region476 – 918443Catalytic
Region532 – 5365Glucose-6-phosphate 2 binding
Region620 – 6212Substrate 2 binding
Region656 – 6572Substrate 2 binding
Region861 – 8633Glucose-6-phosphate 2 binding

Sites

Binding site301ATP 1 By similarity
Binding site1551Substrate 1
Binding site2091Glucose-6-phosphate 1
Binding site2321Glucose-6-phosphate 1
Binding site2351Substrate 1
Binding site2601Substrate 1
Binding site4491Glucose-6-phosphate 1
Binding site6031Glucose-6-phosphate 2
Binding site6571Glucose-6-phosphate 2
Binding site6801ATP 2 By similarity
Binding site6801Glucose-6-phosphate 2
Binding site6831Substrate 2
Binding site7081Substrate 2
Binding site7421Substrate 2
Binding site8971Glucose-6-phosphate 2

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue271Phosphotyrosine By similarity

Secondary structure

1 ..................................................................................................................................... 918
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P05708 [UniParc].

Last modified May 30, 2000. Version 4.
Checksum: D2200820F0FC41EE

FASTA918102,408
        10         20         30         40         50         60 
MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDEILIDIL TRFKKEMKNG LSRDYNPTAS 

        70         80         90        100        110        120 
VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVSMESE IYDTPENIVH 

       130        140        150        160        170        180 
GSGTQLFDHV ADCLGDFMEK KKIKDKKLPV GFTFSFPCRQ SKIDEAVLIT WTKRFKASGV 

       190        200        210        220        230        240 
EGADVVKLLN KAIKKRGDYD ANIVAVVNDT VGTMMTCGYD DQQCEVGLII GTGTNACYME 

       250        260        270        280        290        300 
ELRHIDLVEG DEGRMCINTE WGAFGDDGSL EDIRTEFDRE LDRGSLNPGK QLFEKMVSGM 

       310        320        330        340        350        360 
YMGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKDKEGIQ NAKEILTRLG 

       370        380        390        400        410        420 
VEPSDVDCVS VQHICTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKMH 

       430        440        450        460        470        480 
PQYSRRFHKT LRRLVPDSDV RFLLSESGTG KGAAMVTAVA YRLAEQHRQI EETLAHFRLS 

       490        500        510        520        530        540 
KQTLMEVKKR LRTEMEMGLR KETNSKATVK MLPSFVRSIP DGTEHGDFLA LDLGGTNFRV 

       550        560        570        580        590        600 
LLVKIRSGKK RTVEMHNKIY SIPLEIMQGT GDELFDHIVS CISDFLDYMG IKGPRMPLGF 

       610        620        630        640        650        660 
TFSFPCHQTN LDCGILISWT KGFKATDCEG HDVASLLRDA VKRREEFDLD VVAVVNDTVG 

       670        680        690        700        710        720 
TMMTCAYEEP TCEIGLIVGT GTNACYMEEM KNVEMVEGNQ GQMCINMEWG AFGDNGCLDD 

       730        740        750        760        770        780 
IRTDFDKVVD EYSLNSGKQR FEKMISGMYL GEIVRNILID FTKKGFLFRG QISEPLKTRG 

       790        800        810        820        830        840 
IFETKFLSQI ESDRLALLQV RAILQQLGLN STCDDSILVK TVCGVVSKRA AQLCGAGMAA 

       850        860        870        880        890        900 
VVEKIRENRG LDHLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCTVSF LLSEDGSGKG 

       910 
AALITAVGVR LRGDPSIA

« Hide

References

[1]"Complete amino acid sequence of rat brain hexokinase, deduced from the cloned cDNA, and proposed structure of a mammalian hexokinase."
Schwab D.A., Wilson J.E.
Proc. Natl. Acad. Sci. U.S.A. 86:2563-2567(1989) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1-466.
Tissue: Brain.
[2]"The complete amino acid sequence of the catalytic domain of rat brain hexokinase, deduced from the cloned cDNA."
Schwab D.A., Wilson J.E.
J. Biol. Chem. 263:3220-3224(1988) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE OF 467-918.
Tissue: Brain.
[3]Wilson J.E.
Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[4]"Rat brain hexokinase: amino acid sequence at the substrate hexose binding site is homologous to that of yeast hexokinase."
Schirch D.M., Wilson J.E.
Arch. Biochem. Biophys. 257:1-12(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 597-617; 625-636 AND 802-816.
Tissue: Brain.
[5]White J.A., Liu W., Wilson J.E.
Submitted (DEC-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 1-21.
Strain: Sprague-Dawley.
Tissue: Liver.
[6]White J.A., Wilson J.E.
Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE OF 221-246 AND 631-668.
[7]"Rat brain hexokinase: location of the substrate hexose binding site in a structural domain at the C-terminus of the enzyme."
Schirch D.M., Wilson J.E.
Arch. Biochem. Biophys. 254:385-396(1987) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBSTRATE-BINDING SITE.
[8]"Identification of novel immunodominant epididymal sperm proteins using combinatorial approach."
Khan S.A., Suryawanshi A.R., Ranpura S.A., Jadhav S.V., Khole V.V.
Reproduction 138:81-93(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY, TISSUE SPECIFICITY.
[9]"The structure of mammalian hexokinase-1."
Mulichak A.M., Wilson J.E., Padmanabhan K., Garavito R.M.
Nat. Struct. Biol. 5:555-560(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GLUCOSE AND GLUCOSE-6-PHOSPHATE.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		J04526 mRNA. Translation: AAC20075.1.
U27319 Genomic DNA. Translation: AAC52945.1.
U89160 Genomic DNA. Translation: AAB71376.1.
U89158 Genomic DNA. Translation: AAB71374.1.
IPIIPI00202543.
PIRA32521.
B32521.
C32521.
C59226.
RefSeqNP_036866.1. NM_012734.1.
UniGeneRn.11017.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1BG3X-ray2.80A/B1-918[»]
ProteinModelPortalP05708.
SMRP05708. Positions 1-911.
ModBaseSearch...

PTM databases

PhosphoSiteP05708.

2D gel databases

World-2DPAGE0004:P05708.

Proteomic databases

PRIDEP05708.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID25058.
KEGGrno:25058.

Organism-specific databases

CTD3098.
RGD2796. Hk1.

Phylogenomic databases

HOVERGENHBG005020.
KOK00844.

Enzyme and pathway databases

BRENDA2.7.1.1. 5301.
SABIO-RKP05708.
UniPathwayUPA00242.

Gene expression databases

GenevestigatorP05708.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR022673. Hexokinase_C.
IPR019807. Hexokinase_CS.
IPR022672. Hexokinase_N.
[Graphical view]
PANTHERPTHR19443. PTHR19443. 1 hit.
PfamPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
PROSITEPS00378. HEXOKINASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChEMBLCHEMBL4783.
EvolutionaryTraceP05708.
NextBio605272.

Entry information

Entry nameHXK1_RAT
AccessionPrimary (citable) accession number: P05708
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: May 30, 2000
Last modified: April 3, 2013
This is version 122 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata 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