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Reviewed, UniProtKB/Swiss-Prot Q5RC71 (HXK1_PONAB)

Last modified September 1, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Hexokinase-1
    EC=2.7.1.1
Alternative name(s):
    Hexokinase type I
      Short name=HK I
Gene names
Name: HK1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length917 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at transcript 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 By similarity.

Pathway

Carbohydrate metabolism; hexose metabolism.

Subunit structure

Monomer By similarity.

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 By similarity.

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
   DomainRepeat
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   PTMAcetylation
Phosphoprotein
   Technical termAllosteric enzyme
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 917917Hexokinase-1
PRO_0000286047

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 By similarity
Region172 – 1732Substrate 1 binding By similarity
Region208 – 2092Substrate 1 binding By similarity
Region291 – 2944Substrate 1 binding By similarity
Region413 – 4153Glucose-6-phosphate 1 binding By similarity
Region476 – 917442Catalytic
Region532 – 5365Glucose-6-phosphate 2 binding By similarity
Region603 – 6042Substrate 2 binding By similarity
Region620 – 6212Substrate 2 binding By similarity
Region656 – 6572Substrate 2 binding By similarity
Region861 – 8633Glucose-6-phosphate 2 binding By similarity

Sites

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

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue271Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RC71-1 [UniParc].

Last modified December 21, 2004. Version 1.
Checksum: BCB4765425999C79

FASTA917102,363
        10         20         30         40         50         60 
MIAAQLLAYY FTELKDDQVK KIDKYLYAMR LSDETLIDIM TRFRKEMKNG LSRDFNPTAT 

        70         80         90        100        110        120 
VKMLPTFVRS IPDGSEKGDF IALDLGGSSF RILRVQVNHE KNQNVHMESE VYDTPENIVH 

       130        140        150        160        170        180 
GSGSQLFDHV AECLGDFMEK RKIKDKKSPV GFTFSFPCQQ SKIDEAVLIT WTKRFKASGV 

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

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

       310        320        330        340        350        360 
YLGELVRLIL VKMAKEGLLF EGRITPELLT RGKFNTSDVS AIEKNKEGLH NAKEILTRLG 

       370        380        390        400        410        420 
VEPSDDDCVS VQHVCTIVSF RSANLVAATL GAILNRLRDN KGTPRLRTTV GVDGSLYKTH 

       430        440        450        460        470        480 
PQYSRRFHKT LRRLVPDSDV RFLLSESGSG KGAAMVTAVA YRLAEQHRQI EETLAHFHLT 

       490        500        510        520        530        540 
KDMLLEVKKR MRAEMELGLR KQTHNNAAVK MLPSFVRRTP DGTENGDFLA LDLGGTNFRV 

       550        560        570        580        590        600 
LLVKIRSGKK RTVEMHNKIY AIPIEIMQGT GEELFDHIVS CISDFLDYMG IKGPRMPLGF 

       610        620        630        640        650        660 
TFSFPCKQTS LDAGILITWT KGFKATDCVG NDVATLLRDA IKRREEFDLD VVAVVNDTVG 

       670        680        690        700        710        720 
TMMTCAYEEP TCEVGLIVGT GSNACYMEEM KNVEMVEGDQ GQMCINMEWG AFGDNGCLDD 

       730        740        750        760        770        780 
IRTHYDRLVD EYSLNAGKQR YEKMISGMYL GEIVRNILID FTKKGFLFRG QISEPLKTRG 

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

       850        860        870        880        890        900 
VVDKIRENRG LDRLNVTVGV DGTLYKLHPH FSRIMHQTVK ELSPKCNVSF LLSEDGSGKG 

       910 
AALITAVGVR LRTEASS 

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain cortex.

Cross-references

Sequence databases

CR858409 mRNA. Translation: CAH90636.1.
RefSeqNP_001125344.1.
UniGenePab.19241

3D structure databases

SMRQ5RC71. Positions 16-913.
ModBaseSearch...

Genome annotation databases

GeneID100172246.

Organism-specific databases

CTD100172246.

Phylogenomic databases

HOVERGENQ5RC71.

Enzyme and pathway databases

BRENDA2.7.1.1. 269192.

Family and domain databases

InterProIPR001312. Hexokinase.
IPR019807. Hexokinase_CS.
[Graphical view]
PANTHERPTHR19443. Hexokinase. 1 hit.
PfamPF00349. Hexokinase_1. 2 hits.
PF03727. Hexokinase_2. 2 hits.
[Graphical view]
PRINTSPR00475. HEXOKINASE.
ProDomPD001109. Hexokinase. 2 hits.
[Graphical view] [Entries sharing at least one domain]
PROSITEPS00378. HEXOKINASES. 2 hits.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameHXK1_PONAB
AccessionPrimary (citable) accession number: Q5RC71
Entry history
Integrated into UniProtKB/Swiss-Prot: May 1, 2007
Last sequence update: December 21, 2004
Last modified: September 1, 2009
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents