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Reviewed, UniProtKB/Swiss-Prot Q6FDN3 (GLPK_ACIAD)

Last modified February 9, 2010. Version 51. 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: ACIAD0930
OrganismAcinetobacter sp. (strain ADP1) [Complete proteome] [HAMAP]
Taxonomic identifier62977 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesMoraxellaceaeAcinetobacter

Protein attributes

Sequence length495 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: 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 – 495495Glycerol kinase HAMAP MF_00186
PRO_1000118541

Regions

Nucleotide binding408 – 4125ATP 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
Q6FDN3-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: C429160A95CDC587

FASTA49554,271
        10         20         30         40         50         60 
MSYLLALDQG TTSSRAIIFD EKGQIHATAQ RETRIKTPNS GWVEQDANEI WSSQIAVIQQ 

        70         80         90        100        110        120 
ALASAHILAK DIKALGLTNQ RETTVVWDKR TGKALAPAII WQDRRAAQWC NTLIENGMLV 

       130        140        150        160        170        180 
QVQQKTGLRI DPYFSAGKLV WLLENIAGFR ILAEQGHAAF GTIDSWLVWN LTQGAEHIIE 

       190        200        210        220        230        240 
ASNASRTMLM NLSTQMWDED LLNKFNIPAA ILPKIISSDA YVADTAQGLL GSTIPITGIL 

       250        260        270        280        290        300 
GDQQAALFGQ SCFEVGSAKN TYGTGCFMLF NTGDQLQFSQ NQLLTTLAWQ CQNQTRYALE 

       310        320        330        340        350        360 
GSVFMAGAIV QWLRDGLGLI QHSAQVEQLA SQVQSTEGVV LVPAFTGLGA PHWDSEARAL 

       370        380        390        400        410        420 
LCGMSRGTTK AHIARAALEA IAFQVSDVLC AMQSDLSRPL KELRVDGGAS QNDMLMQFQA 

       430        440        450        460        470        480 
DILNVPVLRP KMLESTAWGA AAMAGLKAGV FTNLDEIAAS WQLDRTFEPK MKNDERESRL 

       490 
CEWSQALKRA KSNLI 

« Hide

References

[1]"Unique features revealed by the genome sequence of Acinetobacter sp. ADP1, a versatile and naturally transformation competent bacterium."
Barbe V., Vallenet D., Fonknechten N., Kreimeyer A., Oztas S., Labarre L., Cruveiller S., Robert C., Duprat S., Wincker P., Ornston L.N., Weissenbach J., Marliere P., Cohen G.N., Medigue C.
Nucleic Acids Res. 32:5766-5779(2004) [PubMed: 15514110] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR543861 Genomic DNA. Translation: CAG67825.1.
RefSeqYP_045647.1.

3D structure databases

HSSPHSSP built from PDB template 1GLJ based on UniProtKB P0A6F3.
SMRQ6FDN3. Positions 3-492.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ6FDN3.

Genome annotation databases

GeneID2879886.
GenomeReviewsGene locus ACIAD0930 in contig CR543861_GR.
KEGGaci:ACIAD0930.
NMPDRfig|62977.3.peg.929.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHBG511469.
OMAKPSSEVY.
PhylomeDBQ6FDN3.

Enzyme and pathway databases

BioCycASP62977:ACIAD0930-MONOMER.

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]
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_ACIAD
AccessionPrimary (citable) accession number: Q6FDN3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: July 19, 2004
Last modified: February 9, 2010
This is version 51 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