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C6C5B9 (C6C5B9_DICDC) Unreviewed, UniProtKB/TrEMBL

Last modified February 19, 2014. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order

Names and origin

Protein namesRecommended name:
Glycerol kinase HAMAP-Rule MF_00186

EC=2.7.1.30 HAMAP-Rule MF_00186
Alternative name(s):
ATP:glycerol 3-phosphotransferase HAMAP-Rule MF_00186
Glycerokinase HAMAP-Rule MF_00186
Gene names
Name:glpK HAMAP-Rule MF_00186
Ordered Locus Names:Dd703_3803 EMBL ACS87556.1
OrganismDickeya dadantii (strain Ech703) [Complete proteome] [HAMAP] EMBL ACS87556.1
Taxonomic identifier579405 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeDickeya

Protein attributes

Sequence length503 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 SAAS SAAS005999

Enzyme regulation

Activity of this regulatory enzyme is affected by several metabolites. Allosterically and non-competitively inhibited by fructose 1,6-bisphosphate (FBP) and unphosphorylated phosphocarrier protein EIIA-Glc (III-Glc), an integral component of the bacterial phosphotransferase (PTS) system 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 SAAS SAAS005999

Subunit structure

Homotetramer and homodimer (in equilibrium). Heterodimer with EIIA-Glc. Binds 1 zinc ion per glycerol kinase EIIA-Glc dimer. The zinc ion is important for dimerization By similarity. HAMAP-Rule MF_00186

Sequence similarities

Belongs to the FGGY kinase family. HAMAP-Rule MF_00186 RuleBase RU003733

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Regions

Nucleotide binding15 – 173ATP By similarity HAMAP-Rule MF_00186
Nucleotide binding413 – 4175ATP By similarity HAMAP-Rule MF_00186
Region85 – 862Substrate binding By similarity HAMAP-Rule MF_00186
Region235 – 2373Allosteric FBP inhibitor binding By similarity HAMAP-Rule MF_00186
Region247 – 2482Substrate binding By similarity HAMAP-Rule MF_00186

Sites

Metal binding4801Zinc; shared with EIIA-Glc By similarity HAMAP-Rule MF_00186
Binding site151Substrate By similarity HAMAP-Rule MF_00186
Binding site191ATP By similarity HAMAP-Rule MF_00186
Binding site1371Substrate By similarity HAMAP-Rule MF_00186
Binding site2691ATP By similarity HAMAP-Rule MF_00186
Binding site3121ATP; via carbonyl oxygen By similarity HAMAP-Rule MF_00186
Binding site3161ATP; via amide nitrogen By similarity HAMAP-Rule MF_00186
Binding site3311ATP By similarity HAMAP-Rule MF_00186

Sequences

Sequence LengthMass (Da)Tools
C6C5B9 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 5825E56251D1F4B5

FASTA50355,776
        10         20         30         40         50         60 
MSQEKKYIVA LDQGTTSSRA VVLDHDANIV SVSQREFPQI YPKPGWVEHD PMEIWASQSS 

        70         80         90        100        110        120 
TLVEALAKAG ISSDEVAGIG ITNQRETVVV WEKETGKPIY NAIVWQCRRT ADICEKLKKD 

       130        140        150        160        170        180 
GLEEYIRANT GLVVDPYFSG TKVKWILDHV DGARDRANRG ELLLGTIDTW LIWKMTQGRV 

       190        200        210        220        230        240 
HVTDYTNASR TMLFNIHKLD WDERMLEALD IPRSMLPQVR PSSEMYGQTN IGGKGGTRIP 

       250        260        270        280        290        300 
ICGIAGDQQA ALYGQLCVQP GMAKNTYGTG CFLLMNTGTE AVASRHGLLT TIACGPRGEV 

       310        320        330        340        350        360 
NYALEGAVFI GGASIQWLRD ELKLINDAAD SEYFATKVKD TNGVYVVPAF TGLGAPYWDP 

       370        380        390        400        410        420 
YARGAIFGLT RGANANHIIR ATLESIAFQT RDVLDAMQAD ADTRLQSLRV DGGAVANNFL 

       430        440        450        460        470        480 
MQFQSDILGT RVERPQVRES TALGAAFLAG LATGFWNDLD EVKSKTAIER EFRPSIETVE 

       490        500 
RNFRYRGWQK AVERARNWED HDA 

« Hide

References

[1]"Complete sequence of Dickeya dadantii Ech703."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H., Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ech703 EMBL ACS87556.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001654 Genomic DNA. Translation: ACS87556.1.
RefSeqYP_002989378.1. NC_012880.1.

3D structure databases

ProteinModelPortalC6C5B9.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING579405.Dd703_3803.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACS87556; ACS87556; Dd703_3803.
GeneID8087188.
KEGGdda:Dd703_3803.
PATRIC21795313. VBIDicDad95084_4030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHOG000222134.
KOK00864.
OMAALYGQLC.
OrthoDBEOG6RZB46.
ProtClustDBCLSK2549748.

Enzyme and pathway databases

BioCycDDAD579405:GHJU-3897-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 nameC6C5B9_DICDC
AccessionPrimary (citable) accession number: C6C5B9
Entry history
Integrated into UniProtKB/TrEMBL: September 1, 2009
Last sequence update: September 1, 2009
Last modified: February 19, 2014
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)