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Protein

Guanylate kinase

Gene

gmk

Organism
Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Essential for recycling GMP and indirectly, cGMP.UniRule annotation

Catalytic activityi

ATP + GMP = ADP + GDP.UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 198ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. guanylate kinase activity Source: UniProtKB-HAMAP

GO - Biological processi

  1. purine nucleotide metabolic process Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciLMON169963:LMO1827-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate kinaseUniRule annotation (EC:2.7.4.8UniRule annotation)
Alternative name(s):
GMP kinaseUniRule annotation
Gene namesi
Name:gmkUniRule annotation
Ordered Locus Names:lmo1827
OrganismiListeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e)
Taxonomic identifieri169963 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesListeriaceaeListeria
ProteomesiUP000000817 Componenti: Chromosome

Organism-specific databases

GenoListiLMO1827.

Subcellular locationi

Cytoplasm UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 205205Guanylate kinasePRO_0000170558Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi169963.lmo1827.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi18 – 2710Combined sources
Beta strandi39 – 424Combined sources
Turni50 – 523Combined sources
Helixi59 – 679Combined sources
Beta strandi71 – 777Combined sources
Beta strandi80 – 856Combined sources
Helixi86 – 949Combined sources
Beta strandi99 – 1024Combined sources
Helixi105 – 11410Combined sources
Beta strandi118 – 1247Combined sources
Turni126 – 1305Combined sources
Helixi144 – 15916Combined sources
Helixi160 – 1623Combined sources
Beta strandi163 – 1686Combined sources
Helixi172 – 18716Combined sources
Helixi190 – 20011Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TAUX-ray2.05A/B1-205[»]
ProteinModelPortaliQ8Y672.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini5 – 184180Guanylate kinase-likeUniRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the guanylate kinase family.UniRule annotation
Contains 1 guanylate kinase-like domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG0194.
HOGENOMiHOG000037639.
KOiK00942.
OMAiMSHYNEY.
OrthoDBiEOG6CP410.
PhylomeDBiQ8Y672.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00328. Guanylate_kinase.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8Y672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTERGLLIVL SGPSGVGKGT VREAVFKDPE TSFDYSISMT TRLPREGEQD
60 70 80 90 100
GVDYYFRSRE VFEQAIKDGK MLEYAEYVGN YYGTPLEYVE EKLAAGVDIF
110 120 130 140 150
LEIEVQGAMQ VRKAMPEGIF IFLTPPDLSE LKNRIIGRGT ESMEVVEERM
160 170 180 190 200
ETAKKEIEMM ASYDYAVVND VVANAVQKIK GIVETEHLKT ERVIHRYKKM

LEGLQ
Length:205
Mass (Da):23,282
Last modified:March 1, 2002 - v1
Checksum:i40579D7F0038C9E1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591981 Genomic DNA. Translation: CAC99905.1.
PIRiAC1303.
RefSeqiNP_465352.1. NC_003210.1.

Genome annotation databases

GeneIDi985464.
KEGGilmo:lmo1827.
PATRICi20312847. VBILisMon69206_1872.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL591981 Genomic DNA. Translation: CAC99905.1.
PIRiAC1303.
RefSeqiNP_465352.1. NC_003210.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3TAUX-ray2.05A/B1-205[»]
ProteinModelPortaliQ8Y672.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi169963.lmo1827.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi985464.
KEGGilmo:lmo1827.
PATRICi20312847. VBILisMon69206_1872.

Organism-specific databases

GenoListiLMO1827.

Phylogenomic databases

eggNOGiCOG0194.
HOGENOMiHOG000037639.
KOiK00942.
OMAiMSHYNEY.
OrthoDBiEOG6CP410.
PhylomeDBiQ8Y672.

Enzyme and pathway databases

BioCyciLMON169963:LMO1827-MONOMER.

Family and domain databases

Gene3Di3.40.50.300. 2 hits.
HAMAPiMF_00328. Guanylate_kinase.
InterProiIPR008145. GK/Ca_channel_bsu.
IPR008144. Guanylate_kin-like.
IPR017665. Guanylate_kinase.
IPR020590. Guanylate_kinase_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00625. Guanylate_kin. 1 hit.
[Graphical view]
SMARTiSM00072. GuKc. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR03263. guanyl_kin. 1 hit.
PROSITEiPS00856. GUANYLATE_KINASE_1. 1 hit.
PS50052. GUANYLATE_KINASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-679 / EGD-e.

Entry informationi

Entry nameiKGUA_LISMO
AccessioniPrimary (citable) accession number: Q8Y672
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: March 1, 2002
Last modified: April 1, 2015
This is version 83 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.