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Reviewed, UniProtKB/Swiss-Prot Q6MJQ2 (GLPK_BDEBA)

Last modified November 3, 2009. Version 38. 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

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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: Bd2718
OrganismBdellovibrio bacteriovorus [Complete proteome] [HAMAP]
Taxonomic identifier959 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Deltaproteobacteria › Bdellovibrionales › Bdellovibrionaceae › Bdellovibrio

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Protein attributes

Sequence length495 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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General annotation (Comments)

Function

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

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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...

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 495495Glycerol kinase HAMAP MF_00186
PRO_1000020703

Regions

Nucleotide binding413 – 4175ATP By similarity

Sites

Binding site141Substrate By similarity
Binding site181ATP By similarity
Binding site841Substrate By similarity
Binding site1361Substrate By similarity
Binding site2461Substrate By similarity
Binding site2681ATP By similarity
Binding site3121ATP; via carbonyl oxygen By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q6MJQ2-1 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: 16003633C9DD0CB6

FASTA49554,309
        10         20         30         40         50         60 
MFMSSFIMAI DQGTTSSRTC IINQAGGLVA EAREAFKQIF PKPGWVEHDP EDIWYSTQRS 

        70         80         90        100        110        120 
MRLALEKAKI KGSQIRTIGI TNQRETVMLW DAKSGKALHN AIVWQCRRTQ DLCEKLKKNK 

       130        140        150        160        170        180 
KEKIITAKTG LVLDPYFSAT KIQWLLKNVP NAAKKAKDGQ ALAGTVDSFL LWKLTAGHSH 

       190        200        210        220        230        240 
KTDVSNASRT MLMNIHTGWW DEDLLKIFGV PEAILPEICP SNSDFGVTQG LGFMPDGIPI 

       250        260        270        280        290        300 
TGIVGDQQAA LFGQTCFETG DSKCTFGTGS FLLLNTGKKA VKSKNKLLTT IAWKLKNQEM 

       310        320        330        340        350        360 
TYALEGGAFV CGAAVQWLRD GLGLIQQSSD VEALAKTVDG TDGVEFVPAL TGLGAPHWQP 

       370        380        390        400        410        420 
EARGLICGLT RGSTKAHIAR ATLEAMALQN VDILNTMQRD LGKKLRGVRV DGGAAANDLL 

       430        440        450        460        470        480 
MQMQADYCGA NVVRPQNLET TALGAAFMAG LGAGVWKDLK EIKRVWKVNK EFKVKMTPKA 

       490 
RKERLQRWAQ ALERV

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References

[1]"A predator unmasked: life cycle of Bdellovibrio bacteriovorus from a genomic perspective."
Rendulic S., Jagtap P., Rosinus A., Eppinger M., Baar C., Lanz C., Keller H., Lambert C., Evans K.J., Goesmann A., Meyer F., Sockett R.E., Schuster S.C.
Science 303:689-692(2004) [PubMed: 14752164] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 15356 / HD100 / DSM 50701 / NCIB 9529.

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Cross-references

Sequence databases

BX842653 Genomic DNA. Translation: CAE80508.1.
RefSeqNP_969515.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2736239.
GenomeReviewsGene locus Bd2718 in contig BX842601_GR.
KEGGbba:Bd2718.
NMPDRfig|264462.1.peg.2487.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6MJQ2.
OMARQTSGIC.

Enzyme and pathway databases

BioCycBBAC264462:BD2718-MON.
BRENDA2.7.1.30. 3459.

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...

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Entry information

Entry nameGLPK_BDEBA
AccessionPrimary (citable) accession number: Q6MJQ2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 5, 2004
Last modified: November 3, 2009
This is version 38 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)

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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