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Reviewed, UniProtKB/Swiss-Prot A1TJR8 (GLPK_ACIAC)

Last modified November 3, 2009. Version 30. 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:
    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: Aave_0602
OrganismAcidovorax avenae subsp. citrulli (strain AAC00-1) [Complete proteome] [HAMAP]
Taxonomic identifier397945 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesComamonadaceaeAcidovorax

Protein attributes

Sequence length506 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism By similarity.

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: HAMAP

   Molecular functionATP binding

Inferred from electronic annotation. Source: HAMAP

glycerol kinase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 506506Glycerol kinase HAMAP MF_00186
PRO_1000098708

Regions

Nucleotide binding421 – 4255ATP 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 site3161ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
A1TJR8-1 [UniParc].

Last modified February 6, 2007. Version 1.
Checksum: 1AEC9DFBD02CEDA8

FASTA50653,912
        10         20         30         40         50         60 
MTYLLALDQG TSSSRSIVFD ERGHIVAQAQ QELPQIYPQP GWVEHDPVDI WRTQIATARQ 

        70         80         90        100        110        120 
ALAQANIGPG DVRALGITNQ RETTVLWNRR TGQPVHHAIV WQDRRAEPLC AELREQGHEP 

       130        140        150        160        170        180 
MIQERTGLRI DAYFSATKLR WLLDQVPGAR AAAEAGELAF GTVDSWLIWQ LTGGKVHVTD 

       190        200        210        220        230        240 
VSNASRTMLF NVHSNDWDDD LLALLRIPRK LLPRVQPSAS DFGATDAALL GGAIPIGGVA 

       250        260        270        280        290        300 
GDQQSALFGQ ACFTAGMAKN TYGTGCFMLM HTGSSFQTSR NGLLTTSAAQ IAPRTGAGHG 

       310        320        330        340        350        360 
APEPAFAMEG SVFVGGAVVQ WLRDGLRAIS SSSEVQSLAE SVPDSGGVMM VPAFTGLGAP 

       370        380        390        400        410        420 
YWKPDARGTI TGLTRGTTIA HIARAALESI AYQSAALLQA MSRDAVAAGG APVSELRVDG 

       430        440        450        460        470        480 
GACVNDLLMQ FQADLLGIPV VRPAVIETTA LGAAYLAGLS SGVYAGTEAL SALWRAERRF 

       490        500 
LPTLSAARAQ ECMARWEHAV RQAALD 

« Hide

References

[1]"Complete sequence of Acidovorax avenae subsp. citrulli AAC00-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Kim E., Stahl D., Richardson P.
Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000512 Genomic DNA. Translation: ABM31206.1.
RefSeqYP_968980.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA1TJR8.

Genome annotation databases

GeneID4668657.
GenomeReviewsGene locus Aave_0602 in contig CP000512_GR.
KEGGaav:Aave_0602.
NMPDRfig|397945.5.peg.518.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMARQTSGIC.

Family and domain databases

HAMAPMF_00186.
[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]
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_ACIAC
AccessionPrimary (citable) accession number: A1TJR8
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: February 6, 2007
Last modified: November 3, 2009
This is version 30 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

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