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Q39V17 (GLPK_GEOMG) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 61. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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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:Gmet_1676
OrganismGeobacter metallireducens (strain GS-15 / ATCC 53774 / DSM 7210) [Complete proteome] [HAMAP]
Taxonomic identifier269799 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Desulfuromonadales › Geobacteraceae › Geobacter ›

Protein attributes

Sequence length496 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Key enzyme in the regulation of glycerol uptake and metabolism By similarity. HAMAP-Rule MF_00186

Catalytic activity

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

Ontologies

Keywords
   Biological processGlycerol metabolism
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processglycerol catabolic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

glycerol-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 – 496496Glycerol kinase HAMAP-Rule MF_00186
PRO_1000098734

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
Q39V17 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 715F4D77D0119A85

FASTA49653,061
        10         20         30         40         50         60 
MSYILALDQG TTSSRAIVFD TTATIRAIAQ REFRQIFPRP GWVEHDGREI WATQVGVAAE 

        70         80         90        100        110        120 
ALTRAGISPR EVRAIGITNQ RETTLLWDRR SGEPLHNAIV WQDRRTAELC DRLKADGLEP 

       130        140        150        160        170        180 
LFRQKTGLVL DAYFSGTKLA WLLEAIPGAR SRAEAGELAF GTVDSWLAWN LSGGKLHVTD 

       190        200        210        220        230        240 
ASNASRTLLF NITTLDWDDE LLAILGIPRA VLPRVVDSGA VYGETAGDIF AAAIPLAGMA 

       250        260        270        280        290        300 
GDQQAALFGQ ACGTAGMAKN TYGTGCFLLM HCGTRPIESR HNLLTTVAWQ LGGRAEYALE 

       310        320        330        340        350        360 
GSVFVAGAAV QWLRDGLGII RSSGEVEALA ASVPDSGGVC LVPAFTGLGA PHWDPYARGT 

       370        380        390        400        410        420 
IVGITRGTTA AHIARATLES IAFQSADLLT AMEADAGISL AELRVDGGAT ANGLLMQFQA 

       430        440        450        460        470        480 
DLLGVPVVRP RISETTALGA AYLAGLAVGL WRDRQEIAGH WQVDRIFEPA MGREQAAELR 

       490 
GRWGRAVERA RGWAAP

« Hide

References

[1]"Complete sequence of Geobacter metallireducens GS-15."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Di Bartolo G., Chain P., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
Submitted (OCT-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GS-15 / ATCC 53774 / DSM 7210.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000148 Genomic DNA. Translation: ABB31907.1.
RefSeqYP_006720643.1. NC_007517.1.

3D structure databases

ProteinModelPortalQ39V17.
SMRQ39V17. Positions 3-494.
ModBaseSearch...

Protein-protein interaction databases

STRING269799.Gmet_1676.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABB31907; ABB31907; Gmet_1676.
GeneID3740526.
KEGGgme:Gmet_1676.
PATRIC22002580. VBIGeoMet55070_1715.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHOG000222134.
KOK00864.
OMALANAVQC.
ProtClustDBCLSK743164.

Enzyme and pathway databases

BioCycGMET269799:GHNY-1703-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]
PANTHERPTHR10196:SF9. PTHR10196:SF9. 1 hit.
PfamPF02782. FGGY_C. 1 hit.
PF00370. FGGY_N. 1 hit.
[Graphical view]
TIGRFAMsTIGR01311. glycerol_kin. 1 hit.
PROSITEPS00933. FGGY_KINASES_1. False negative.
PS00445. FGGY_KINASES_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGLPK_GEOMG
AccessionPrimary (citable) accession number: Q39V17
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 22, 2005
Last modified: May 29, 2013
This is version 61 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

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