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Protein

Guanylate kinase

Gene

GUK1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Essential for recycling GMP and indirectly, cGMP.

Miscellaneous

Present with 20500 molecules/cell in log phase SD medium.1 Publication

Catalytic activityi

ATP + GMP = ADP + GDP.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi9 – 16ATP8
Nucleotide bindingi35 – 82GMPAdd BLAST48

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • guanylate kinase activity Source: SGD

GO - Biological processi

  • GDP biosynthetic process Source: SGD
  • purine nucleotide metabolic process Source: UniProtKB

Keywordsi

Molecular functionKinase, Transferase
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER3O-102
YEAST:MONOMER3O-102
BRENDAi2.7.4.8 984
ReactomeiR-SCE-451308 Activation of Ca-permeable Kainate Receptor
R-SCE-499943 Interconversion of nucleotide di- and triphosphates
R-SCE-5625900 RHO GTPases activate CIT

Names & Taxonomyi

Protein namesi
Recommended name:
Guanylate kinase (EC:2.7.4.8)
Alternative name(s):
GMP kinase
Gene namesi
Name:GUK1
Ordered Locus Names:YDR454C
ORF Names:D9461.39
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome IV

Organism-specific databases

EuPathDBiFungiDB:YDR454C
SGDiS000002862 GUK1

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cell wall Cytoskeleton Vacuole Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001706552 – 187Guanylate kinaseAdd BLAST186

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylserine2 Publications1
Modified residuei149PhosphoserineCombined sources1
Modified residuei157PhosphotyrosineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP15454
PaxDbiP15454
PRIDEiP15454
TopDownProteomicsiP15454

PTM databases

iPTMnetiP15454

Interactioni

Subunit structurei

Monomer.

Protein-protein interaction databases

BioGridi32509, 187 interactors
DIPiDIP-6721N
IntActiP15454, 2 interactors
MINTiP15454
STRINGi4932.YDR454C

Structurei

Secondary structure

1187
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi5 – 8Combined sources4
Helixi15 – 25Combined sources11
Turni27 – 29Combined sources3
Beta strandi30 – 32Combined sources3
Beta strandi35 – 37Combined sources3
Turni47 – 49Combined sources3
Beta strandi50 – 53Combined sources4
Helixi56 – 64Combined sources9
Beta strandi68 – 74Combined sources7
Beta strandi77 – 82Combined sources6
Helixi83 – 92Combined sources10
Beta strandi94 – 99Combined sources6
Helixi102 – 109Combined sources8
Helixi112 – 114Combined sources3
Beta strandi117 – 122Combined sources6
Helixi126 – 136Combined sources11
Helixi141 – 158Combined sources18
Turni159 – 161Combined sources3
Beta strandi163 – 168Combined sources6
Helixi172 – 183Combined sources12

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1EX6X-ray2.30A/B2-187[»]
1EX7X-ray1.90A2-187[»]
1GKYX-ray2.00A2-187[»]
4F4JX-ray2.45A/B1-187[»]
ProteinModelPortaliP15454
SMRiP15454
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15454

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini2 – 184Guanylate kinase-likeAdd BLAST183

Sequence similaritiesi

Belongs to the guanylate kinase family.Curated

Phylogenomic databases

GeneTreeiENSGT00760000118866
HOGENOMiHOG000037640
InParanoidiP15454
KOiK00942
OMAiAGNYYGT
OrthoDBiEOG092C4CZ3

Family and domain databases

HAMAPiMF_00328 Guanylate_kinase, 1 hit
InterProiView protein in InterPro
IPR008145 GK/Ca_channel_bsu
IPR008144 Guanylate_kin-like_dom
IPR017665 Guanylate_kinase
IPR020590 Guanylate_kinase_CS
IPR027417 P-loop_NTPase
PfamiView protein in Pfam
PF00625 Guanylate_kin, 1 hit
SMARTiView protein in SMART
SM00072 GuKc, 1 hit
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR03263 guanyl_kin, 1 hit
PROSITEiView protein in PROSITE
PS00856 GUANYLATE_KINASE_1, 1 hit
PS50052 GUANYLATE_KINASE_2, 1 hit

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P15454-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSRPIVISGP SGTGKSTLLK KLFAEYPDSF GFSVSSTTRT PRAGEVNGKD
60 70 80 90 100
YNFVSVDEFK SMIKNNEFIE WAQFSGNYYG STVASVKQVS KSGKTCILDI
110 120 130 140 150
DMQGVKSVKA IPELNARFLF IAPPSVEDLK KRLEGRGTET EESINKRLSA
160 170 180
AQAELAYAET GAHDKVIVND DLDKAYKELK DFIFAEK
Length:187
Mass (Da):20,637
Last modified:January 23, 2007 - v2
Checksum:i5DC4D2A22594BFB8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L04683 Genomic DNA Translation: AAA34657.1
U33007 Genomic DNA Translation: AAB64881.1
BK006938 Genomic DNA Translation: DAA12289.1
PIRiA45097 KIBYGU
RefSeqiNP_010742.1, NM_001180762.1

Genome annotation databases

EnsemblFungiiYDR454C; YDR454C; YDR454C
GeneIDi852065
KEGGisce:YDR454C

Similar proteinsi

Entry informationi

Entry nameiKGUA_YEAST
AccessioniPrimary (citable) accession number: P15454
Secondary accession number(s): D6VT79
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: January 23, 2007
Last modified: May 23, 2018
This is version 188 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome
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Main funding by: National Institutes of Health