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Reviewed, UniProtKB/Swiss-Prot Q81GZ2 (GLPK_BACCR)

Last modified February 9, 2010. Version 46. 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: BC_1035
OrganismBacillus cereus (strain ATCC 14579 / DSM 31) [Complete proteome] [HAMAP]
Taxonomic identifier226900 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillusBacillus cereus group

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. 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 – 496496Glycerol kinase HAMAP MF_00186
PRO_0000059432

Regions

Nucleotide binding410 – 4145ATP By similarity

Sites

Binding site121Substrate By similarity
Binding site161ATP By similarity
Binding site821Substrate By similarity
Binding site1341Substrate By similarity
Binding site2441Substrate By similarity
Binding site2661ATP By similarity
Binding site3091ATP; via carbonyl oxygen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q81GZ2-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: FA9425A595375B6F

FASTA49655,118
        10         20         30         40         50         60 
MKKYILSLDQ GTTSSRAILF NKKGEIVHSA QKEFTQHFPK PGWVEHNAQE IWGSILAVIA 

        70         80         90        100        110        120 
TCLSEADVKP EQIAGIGITN QRETTVVWDK TTSKPIYNAI VWQSRQTAEI CDELKEKGYS 

       130        140        150        160        170        180 
EMVREKTGLL IDAYFSGTKV KWILDNVEGA REKAENGDLL FGTIDSWLVW KLSGGKAHVT 

       190        200        210        220        230        240 
DYSNASRTLM FNIHDLQWDD ELLEMLTVPK SMLPEVRPSS EIYGETIDYH FFGQNVPIAG 

       250        260        270        280        290        300 
VAGDQQAALF GQACFGEGMA KNTYGTGCFM LMNTGEKAVA SEHGLLTTIA WGIDGKVNYA 

       310        320        330        340        350        360 
LEGSIFVAGS AIQWLRDGMR MFKDASESEV YASRVESTDG VYVVPAFVGL GTPYWDSEVR 

       370        380        390        400        410        420 
GAMFGVTRGT TKEHFIRATL ESLAYQTKDV LCAMEADSGI ELKTLRVDGG AVKNNFLMKF 

       430        440        450        460        470        480 
QSDILDVPVE RPVINETTAL GAAYLAGLAV GYWKNQDEIK EQWHMDKRFE PTMEAKTSEE 

       490 
LYAGWKKAIE ATKAFK 

« Hide

References

[1]"Genome sequence of Bacillus cereus and comparative analysis with Bacillus anthracis."
Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V., Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M., Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G. expand/collapse author list , Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.
Nature 423:87-91(2003) [PubMed: 12721630] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE016877 Genomic DNA. Translation: AAP08022.1.
RefSeqNP_830821.1.

3D structure databases

SMRQ81GZ2. Positions 4-489.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ81GZ2.

Genome annotation databases

GeneID1203384.
GenomeReviewsGene locus BC_1035 in contig AE016877_GR.
KEGGbce:BC1035.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0554.
HOGENOMHBG511469.
OMAKPSSEVY.

Enzyme and pathway databases

BioCycBCER226900:BC_1035-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_BACCR
AccessionPrimary (citable) accession number: Q81GZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: June 1, 2003
Last modified: February 9, 2010
This is version 46 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