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B3QH88 (GLPK_RHOPT) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 40. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
Glycerol kinase

EC=2.7.1.30
Alternative name(s):
ATP:glycerol 3-phosphotransferase
Glycerokinase
Short name=GK
Gene names
Name:glpK
Ordered Locus Names:Rpal_4226
OrganismRhodopseudomonas palustris (strain TIE-1) [Complete proteome] [HAMAP]
Taxonomic identifier395960 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length500 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism. Catalyzes the phosphorylation of glycerol to yield sn-glycerol 3-phosphate By similarity. HAMAP-Rule MF_00186

Catalytic activity

ATP + glycerol = ADP + sn-glycerol 3-phosphate. HAMAP-Rule MF_00186

Enzyme regulation

Inhibited by fructose 1,6-bisphosphate (FBP) By similarity. HAMAP-Rule MF_00186

Pathway

Polyol metabolism; glycerol degradation via glycerol kinase pathway; sn-glycerol 3-phosphate from glycerol: step 1/1. HAMAP-Rule MF_00186

Sequence similarities

Belongs to the FGGY kinase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Glycerol kinase HAMAP-Rule MF_00186
PRO_1000098753

Regions

Nucleotide binding11 – 133ATP By similarity
Nucleotide binding411 – 4155ATP By similarity
Region81 – 822Substrate binding By similarity
Region242 – 2432Substrate binding By similarity

Sites

Binding site111Substrate By similarity
Binding site151ATP By similarity
Binding site1331Substrate By similarity
Binding site2641ATP By similarity
Binding site3071ATP; via carbonyl oxygen By similarity
Binding site3111ATP; via amide nitrogen By similarity
Binding site3261ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
B3QH88 [UniParc].

Last modified September 2, 2008. Version 1.
Checksum: 384BA6073C542196

FASTA50053,761
        10         20         30         40         50         60 
MPFVMAIDQG TTSSRAILFR SDISIAASAQ QEFPQHFPAS GWVEHEPEDI WATTIATCRA 

        70         80         90        100        110        120 
AMDKAGATAA DIAAIGITNQ RETVVVWDAV SGQAIHRAIV WQDRRTAEFC TRLKAEGLEP 

       130        140        150        160        170        180 
MVTAKTGLII DPYFSGTKVA WLLDNVPGAR ARAERGELKF GTVDCYLLWR LTGGKVHATD 

       190        200        210        220        230        240 
ATNASRTLLF NIHDGAWDDE LLKLLGVPRS MLPEVKDSSA HFGDSVPELF GGSITIRGIA 

       250        260        270        280        290        300 
GDQQAATIGQ ACFTPGMIKS TYGTGCFALL NTGATPVKSN NKLLTTVAYQ LGGKRTYALE 

       310        320        330        340        350        360 
GSIFVAGSAV QWLRDGLGVI KHASETGPLA DKSDSAQSVY LVPAFVGMGA PYWNPRVRGA 

       370        380        390        400        410        420 
LFGLTRNTGP AELAHAALES VCYQTFDLWA AMRADWPDAD AATTVLRVDG GMTASDWTMQ 

       430        440        450        460        470        480 
RLADLLDAPV DRPVIQETTA LGAAYLAGLS AGVFPEPQKF ADNWRLDHRF RPAMSAATRE 

       490        500 
RKLAGWARAV RGLLATDEGE 

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris TIE-1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Emerson D., Newman D.K., Roden E., Richardson P.
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: TIE-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001096 Genomic DNA. Translation: ACF02722.1.
RefSeqYP_001993197.1. NC_011004.1.

3D structure databases

ProteinModelPortalB3QH88.
SMRB3QH88. Positions 3-494.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING395960.Rpal_4226.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACF02722; ACF02722; Rpal_4226.
GeneID6411910.
KEGGrpt:Rpal_4226.
PATRIC23312959. VBIRhoPal88240_4270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHOG000222134.
KOK00864.
OMAHFFGVEV.
OrthoDBEOG6RZB46.

Enzyme and pathway databases

BioCycRPAL395960:GHPC-4269-MONOMER.
UniPathwayUPA00618; UER00672.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
InterProIPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. 1 hit.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPK_RHOPT
AccessionPrimary (citable) accession number: B3QH88
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: September 2, 2008
Last modified: May 14, 2014
This is version 40 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

PATHWAY comments

Index of metabolic and biosynthesis pathways