Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

O58328 (GLKA_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 85. 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:
ADP-dependent glucokinase

Short name=ADP-GK
Short name=ADPGK
EC=2.7.1.147
Gene names
Name:glkA
Ordered Locus Names:PH0589
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the phosphorylation of D-glucose to D-glucose 6-phosphate using ADP as the phosphate donor. HAMAP-Rule MF_00809

Catalytic activity

ADP + D-glucose = AMP + D-glucose 6-phosphate. HAMAP-Rule MF_00809

Cofactor

Binds 1 magnesium ion per subunit By similarity. HAMAP-Rule MF_00809

Pathway

Carbohydrate degradation; glycolysis. HAMAP-Rule MF_00809

Subunit structure

Monomer.

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00809.

Sequence similarities

Belongs to the ADP-dependent glucokinase family.

Contains 1 ADPK (ADP-dependent kinase) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Glucose metabolism
Glycolysis
   Cellular componentCytoplasm
   LigandMagnesium
Metal-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological_processglycolysis

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionADP-specific glucokinase activity

Inferred from electronic annotation. Source: UniProtKB-EC

glucokinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457ADP-dependent glucokinase HAMAP-Rule MF_00809
PRO_0000184773

Regions

Domain5 – 457453ADPK
Nucleotide binding345 – 3473ADP By similarity
Nucleotide binding441 – 4455ADP By similarity

Sites

Active site4431Proton acceptor By similarity
Metal binding2691Magnesium By similarity
Metal binding2981Magnesium By similarity
Metal binding4431Magnesium By similarity
Binding site331Glucose By similarity
Binding site371Glucose By similarity
Binding site911Glucose By similarity
Binding site1161Glucose By similarity
Binding site1791Glucose By similarity
Binding site2001Glucose By similarity
Binding site2951ADP By similarity
Binding site3451ADP By similarity
Binding site3461ADP; via carbonyl oxygen By similarity
Binding site4321ADP; via carbonyl oxygen By similarity
Binding site4431ADP By similarity
Binding site4431Glucose By similarity

Secondary structure

.............................................................................. 457
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O58328 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A30EF1398FA9BC94

FASTA45752,090
        10         20         30         40         50         60 
MITMTNWESL YEKALDKVEA SIRKVRGVLL AYNTNIDAIK YLKREDLEKR IEKVGKEEVL 

        70         80         90        100        110        120 
RYSEELPKEI ETIPQLLGSI LWSIKRGKAA ELLVVSREVR EYMRKWGWDE LRMGGQVGIM 

       130        140        150        160        170        180 
ANLLGGVYGI PVIAHVPQLS ELQASLFLDG PIYVPTFERG ELRLIHPREF RKGEEDCIHY 

       190        200        210        220        230        240 
IYEFPRNFKV LDFEAPRENR FIGAADDYNP ILYVREEWIE RFEEIAKRSE LAIISGLHPL 

       250        260        270        280        290        300 
TQENHGKPIK LVREHLKILN DLGIRAHLEF AFTPDEVVRL EIVKLLKHFY SVGLNEVELA 

       310        320        330        340        350        360 
SVVSVMGEKE LAERIISKDP ADPIAVIEGL LKLIKETGVK RIHFHTYGYY LALTREKGEH 

       370        380        390        400        410        420 
VRDALLFSAL AAATKAMKGN IEKLSDIREG LAVPIGEQGL EVEKILEKEF SLRDGIGSIE 

       430        440        450 
DYQLTFIPTK VVKKPKSTVG IGDTISSSAF VSEFSLH 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequence and gene organization of the genome of a hyper-thermophilic archaebacterium, Pyrococcus horikoshii OT3."
Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S., Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K., Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T. expand/collapse author list , Tanaka T., Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T., Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.
DNA Res. 5:55-76(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
[2]"Crystal structure of the ADP-dependent glucokinase from Pyrococcus horikoshii at 2.0-A resolution: a large conformational change in ADP-dependent glucokinase."
Tsuge H., Sakuraba H., Kobe T., Kujime A., Katunuma N., Ohshima T.
Protein Sci. 11:2456-2463(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA29678.1.
PIRA71174.
RefSeqNP_142553.1. NC_000961.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1L2LX-ray2.00A1-457[»]
ProteinModelPortalO58328.
SMRO58328. Positions 7-457.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH0589.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA29678; BAA29678; BAA29678.
GeneID1442924.
KEGGpho:PH0589.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG4809.
HOGENOMHOG000254055.
KOK00918.
OMALAYNTNI.
ProtClustDBPRK14038.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-585-MONOMER.
UniPathwayUPA00109.

Family and domain databases

HAMAPMF_00809. ADP_glucokinase.
InterProIPR007666. ADP_PFK/GK.
IPR015990. ADP_PFK/GK_arc.
[Graphical view]
PANTHERPTHR21208. PTHR21208. 1 hit.
PfamPF04587. ADP_PFK_GK. 1 hit.
[Graphical view]
PIRSFPIRSF015883. ADP-Pfk_glckin. 1 hit.
PROSITEPS51255. ADPK. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceO58328.

Entry information

Entry nameGLKA_PYRHO
AccessionPrimary (citable) accession number: O58328
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2005
Last sequence update: August 1, 1998
Last modified: April 16, 2014
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways