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Q65JT0 (KGUA_BACLD) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Guanylate kinase

EC=2.7.4.8
Alternative name(s):
GMP kinase
Gene names
Name:gmk
Ordered Locus Names:BLi01789, BL02293
OrganismBacillus licheniformis (strain DSM 13 / ATCC 14580) [Complete proteome] [HAMAP]
Taxonomic identifier279010 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus

Protein attributes

Sequence length204 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Essential for recycling GMP and indirectly, cGMP By similarity. HAMAP-Rule MF_00328

Catalytic activity

ATP + GMP = ADP + GDP. HAMAP-Rule MF_00328

Subcellular location

Cytoplasm By similarity HAMAP-Rule MF_00328.

Sequence similarities

Belongs to the guanylate kinase family.

Contains 1 guanylate kinase-like domain.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processpurine nucleotide metabolic process

Inferred from electronic annotation. Source: UniProtKB-HAMAP

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

guanylate kinase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 204204Guanylate kinase HAMAP-Rule MF_00328
PRO_0000266288

Regions

Domain5 – 184180Guanylate kinase-like
Nucleotide binding12 – 198ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q65JT0 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: D39E17632B99BCBC

FASTA20423,469
        10         20         30         40         50         60 
MKERGLLIVL SGPSGVGKGT VRQALFAQED TKFEYSISVT TRKPRQGERD GVDYFFKTRE 

        70         80         90        100        110        120 
EFEEMIENNK LLEWAEYVGN YYGTPVDYVE QTLESGRDVF LEIEVQGALQ VRKAFPEGLF 

       130        140        150        160        170        180 
IFLAPPSLAE LKNRIVTRGT ETEATIENRM KAAKEEIELM DAYDYVVEND SIELACERIK 

       190        200 
AIVLAEHLRR DRVAPRYKKM LEVE 

« Hide

References

[1]"The complete genome sequence of Bacillus licheniformis DSM13, an organism with great industrial potential."
Veith B., Herzberg C., Steckel S., Feesche J., Maurer K.H., Ehrenreich P., Baeumer S., Henne A., Liesegang H., Merkl R., Ehrenreich A., Gottschalk G.
J. Mol. Microbiol. Biotechnol. 7:204-211(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.
[2]"Complete genome sequence of the industrial bacterium Bacillus licheniformis and comparisons with closely related Bacillus species."
Rey M.W., Ramaiya P., Nelson B.A., Brody-Karpin S.D., Zaretsky E.J., Tang M., Lopez de Leon A., Xiang H., Gusti V., Clausen I.G., Olsen P.B., Rasmussen M.D., Andersen J.T., Joergensen P.L., Larsen T.S., Sorokin A., Bolotin A., Lapidus A. expand/collapse author list , Galleron N., Ehrlich S.D., Berka R.M.
Genome Biol. 5:R77.1-R77.12(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 13 / ATCC 14580.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017333 Genomic DNA. Translation: AAU40684.1.
CP000002 Genomic DNA. Translation: AAU23324.2.
RefSeqYP_006713165.1. NC_006322.1.
YP_078962.2. NC_006270.3.

3D structure databases

ProteinModelPortalQ65JT0.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING279010.BL02293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAU23324; AAU23324; BL02293.
AAU40684; AAU40684; BLi01789.
GeneID3030944.
3098229.
KEGGbld:BLi01789.
bli:BL02293.
PATRIC18949179. VBIBacLic203714_1793.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0194.
HOGENOMHOG000037639.
KOK00942.
OMAMSHYNEY.
OrthoDBEOG6CP410.

Enzyme and pathway databases

BioCycBLIC279010:GJ2P-1774-MONOMER.

Family and domain databases

Gene3D3.40.50.300. 2 hits.
HAMAPMF_00328. Guanylate_kinase.
InterProIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR03263. guanyl_kin. 1 hit.
PROSITEPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameKGUA_BACLD
AccessionPrimary (citable) accession number: Q65JT0
Secondary accession number(s): Q62V85
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: October 25, 2004
Last modified: May 14, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families