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B3QH88 (GLPK_RHOPT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 25. 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 By similarity. HAMAP MF_00186

Catalytic activity

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

Pathway

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

Sequence similarities

Belongs to the FGGY kinase family.

Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processglycerol-3-phosphate metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

glycerol kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 500500Glycerol kinase HAMAP MF_00186
PRO_1000098753

Regions

Nucleotide binding411 – 4155ATP By similarity

Sites

Binding site111Substrate By similarity
Binding site151ATP By similarity
Binding site811Substrate By similarity
Binding site1331Substrate By similarity
Binding site2421Substrate By similarity
Binding site2641ATP By similarity
Binding site3071ATP; via carbonyl oxygen 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...

Protein-protein interaction databases

STRINGB3QH88.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6411910.
GenomeReviewsGene locus Rpal_4226 in contig CP001096_GR.
KEGGrpt:Rpal_4226.
PATRIC23312959. VBIRhoPal88240_4270.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG511469.
OMACYQTRDL.
ProtClustDBCLSK818559.

Family and domain databases

HAMAPMF_00186. Glycerol_kin.
[Tree]
InterProIPR000577. Carb_kinase_FGGY.
IPR018485. Carb_kinase_FGGY_C.
IPR018483. Carb_kinase_FGGY_CS.
IPR018484. Carb_kinase_FGGY_N.
IPR005999. Glycerol_kin.
[Graphical view]
KOK00864.
PANTHERPTHR10196. FGGY_kin. 1 hit.
PTHR10196:SF9. Glycerol_kin. 1 hit.
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: January 25, 2012
This is version 25 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families