Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot O58328 (GLKA_PYRHO)

Last modified November 3, 2009. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
    ADP-dependent glucokinase
      Short name=ADPGK
      Short name=ADP-GK
    EC=2.7.1.147
Gene names
Name: glkA
Ordered Locus Names: PH0589
OrganismPyrococcus horikoshii [Complete proteome] [HAMAP]
Taxonomic identifier53953 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length457 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 MF_00809

Catalytic activity

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

Cofactor

Binds 1 magnesium ion per subunit By similarity.

Pathway

Carbohydrate degradation; glycolysis. HAMAP MF_00809

Subunit structure

Monomer. HAMAP MF_00809

Subcellular location

Cytoplasm Probable.

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: HAMAP

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionADP-specific glucokinase activity

Inferred from electronic annotation. Source: EC

glucokinase activity

Inferred from electronic annotation. Source: HAMAP

magnesium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 457457ADP-dependent glucokinase HAMAP 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
O58328-1 [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: 9679194] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: OT3.
[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: 12237466] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
Strain: OT3.

Cross-references

Sequence databases

BA000001 Genomic DNA. Translation: BAA29678.1.
PIRA71174.
RefSeqNP_142553.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1L2LX-ray2.00A1-457[»]
ModBaseSearch...

Genome annotation databases

GeneID1442924.
GenomeReviewsGene locus PH0589 in contig BA000001_GR.
KEGGpho:PH0589.
NMPDRfig|70601.1.peg.577.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMO58328.
OMAGIMANLL.

Enzyme and pathway databases

BRENDA2.7.1.147. 74679.

Family and domain databases

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

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: November 3, 2009
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

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

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