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Protein

Uridylate kinase

Gene

URA6

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

Functioni

Catalyzes the phosphorylation of pyrimidine nucleoside monophosphates at the expense of ATP. Plays an important role in de novo pyrimidine nucleotide biosynthesis. Has preference for UMP and dUMP as phosphate acceptors, but can also use CMP, dCMP, AMP, GMP, dGMP and dTMP. ATP and dATP are the best phosphate donors, but can also use GTP, dGTP, dCTP, and dTTP to some degree.UniRule annotation4 Publications

Miscellaneous

Present with 1500 molecules/cell in log phase SD medium.1 Publication

Caution

There is controversy about the substrate specificity of the enzyme. Next to the primary substrate UMP, PubMed:1333436 and Ref. 8 report that the enzyme accepts also CMP and AMP as nucleoside monophosphates, but not GMP, whereas PubMed:2172245 and PubMed:8391780 report activity with GMP and dTMP, but not AMP or CMP.4 Publications

Catalytic activityi

ATP + UMP = ADP + UDP.UniRule annotation5 Publications

Cofactori

Mg2+UniRule annotation2 PublicationsNote: Binds 1 Mg2+ ion per monomer.UniRule annotation2 Publications

Kineticsi

  1. KM=0.15 mM for UMP1 Publication
  2. KM=1.0 mM for dUMP1 Publication
  3. KM=1.8 mM for dTMP1 Publication
  4. KM=0.11 mM for ATP1 Publication
  5. KM=0.53 mM for dCMP1 Publication
  1. Vmax=120 µmol/min/mg enzyme (for dCDP synthesis)1 Publication

pH dependencei

Optimum pH is 6-9.5.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei52NMPUniRule annotation2 Publications1
Binding sitei111NMPUniRule annotation2 Publications1
Binding sitei142ATPUniRule annotation2 Publications1
Binding sitei148NMPUniRule annotation2 Publications1
Binding sitei159NMPUniRule annotation2 Publications1
Binding sitei187ATP; via carbonyl oxygenUniRule annotation2 Publications1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi26 – 31ATPUniRule annotation2 Publications6
Nucleotide bindingi74 – 76NMPUniRule annotation2 Publications3
Nucleotide bindingi104 – 107NMPUniRule annotation2 Publications4

GO - Molecular functioni

  • adenylate kinase activity Source: SGD
  • ATP binding Source: UniProtKB-KW
  • cytidylate kinase activity Source: UniProtKB-EC
  • uridylate kinase activity Source: SGD

GO - Biological processi

  • 'de novo' pyrimidine nucleobase biosynthetic process Source: SGD
  • nucleobase-containing compound metabolic process Source: SGD
  • pyrimidine nucleotide biosynthetic process Source: UniProtKB-KW

Keywordsi

Molecular functionKinase, Transferase
Biological processPyrimidine biosynthesis
LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciMetaCyc:YKL024C-MONOMER
YEAST:YKL024C-MONOMER
BRENDAi2.7.4.B1 984
ReactomeiR-SCE-499943 Interconversion of nucleotide di- and triphosphates

Names & Taxonomyi

Protein namesi
Recommended name:
Uridylate kinaseUniRule annotation (EC:2.7.4.14UniRule annotation)
Short name:
UKUniRule annotation
Alternative name(s):
ATP:UMP phosphotransferaseUniRule annotation
Deoxycytidylate kinaseUniRule annotation
Short name:
CKUniRule annotation
Short name:
dCMP kinaseUniRule annotation
Suppressor of cdc8 protein
Uridine monophosphate kinaseUniRule annotation
Short name:
UMP kinaseUniRule annotation
Short name:
UMPKUniRule annotation
Gene namesi
Name:URA6UniRule annotation
Synonyms:SOC8
Ordered Locus Names:YKL024C
OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Taxonomic identifieri559292 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
Proteomesi
  • UP000002311 Componenti: Chromosome XI

Organism-specific databases

EuPathDBiFungiDB:YKL024C
SGDiS000001507 URA6

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi29K → E: Abolishes catalytic activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001589471 – 204Uridylate kinaseAdd BLAST204

Proteomic databases

MaxQBiP15700
PaxDbiP15700
PRIDEiP15700

Interactioni

Subunit structurei

Monomer.UniRule annotation3 Publications

Protein-protein interaction databases

BioGridi34107, 229 interactors
DIPiDIP-4756N
IntActiP15700, 1 interactor
MINTiP15700
STRINGi4932.YKL024C

Structurei

Secondary structure

1204
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Turni13 – 15Combined sources3
Beta strandi17 – 22Combined sources6
Helixi29 – 39Combined sources11
Beta strandi43 – 46Combined sources4
Helixi47 – 56Combined sources10
Helixi63 – 71Combined sources9
Helixi78 – 94Combined sources17
Beta strandi99 – 103Combined sources5
Helixi109 – 118Combined sources10
Beta strandi123 – 129Combined sources7
Helixi132 – 146Combined sources15
Helixi153 – 165Combined sources13
Helixi168 – 175Combined sources8
Turni176 – 178Combined sources3
Beta strandi180 – 184Combined sources5
Helixi189 – 203Combined sources15

3D structure databases

ProteinModelPortaliP15700
SMRiP15700
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP15700

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni46 – 76NMPbindUniRule annotation2 PublicationsAdd BLAST31
Regioni141 – 151LIDUniRule annotation2 PublicationsAdd BLAST11

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.UniRule annotation2 Publications

Sequence similaritiesi

Belongs to the adenylate kinase family. UMP-CMP kinase subfamily.UniRule annotation

Phylogenomic databases

GeneTreeiENSGT00390000016215
HOGENOMiHOG000238771
InParanoidiP15700
KOiK13800
OMAiFCHLSAG
OrthoDBiEOG092C5OQU

Family and domain databases

CDDicd01428 ADK, 1 hit
HAMAPiMF_00235 Adenylate_kinase_Adk, 1 hit
MF_03172 Adenylate_kinase_UMP_CMP_kin, 1 hit
InterProiView protein in InterPro
IPR000850 Adenylat/UMP-CMP_kin
IPR033690 Adenylat_kinase_CS
IPR027417 P-loop_NTPase
IPR006266 UMP_CMP_kinase
PANTHERiPTHR23359 PTHR23359, 1 hit
PRINTSiPR00094 ADENYLTKNASE
SUPFAMiSSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR01359 UMP_CMP_kin_fam, 1 hit
PROSITEiView protein in PROSITE
PS00113 ADENYLATE_KINASE, 1 hit

Sequencei

Sequence statusi: Complete.

P15700-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTAATTSQPA FSPDQVSVIF VLGGPGAGKG TQCEKLVKDY SFVHLSAGDL
60 70 80 90 100
LRAEQGRAGS QYGELIKNCI KEGQIVPQEI TLALLRNAIS DNVKANKHKF
110 120 130 140 150
LIDGFPRKMD QAISFERDIV ESKFILFFDC PEDIMLERLL ERGKTSGRSD
160 170 180 190 200
DNIESIKKRF NTFKETSMPV IEYFETKSKV VRVRCDRSVE DVYKDVQDAI

RDSL
Length:204
Mass (Da):22,933
Last modified:April 1, 1990 - v1
Checksum:iDDD7645EBCF4088D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M31455 Genomic DNA Translation: AAA35194.1
M69295 Genomic DNA Translation: AAA35200.1
Z28024 Genomic DNA Translation: CAA81859.1
AY558074 Genomic DNA Translation: AAS56400.1
BK006944 Genomic DNA Translation: DAA09130.1
PIRiA33572
RefSeqiNP_012901.3, NM_001179590.3

Genome annotation databases

EnsemblFungiiYKL024C; YKL024C; YKL024C
GeneIDi853844
KEGGisce:YKL024C

Similar proteinsi

Entry informationi

Entry nameiKCY_YEAST
AccessioniPrimary (citable) accession number: P15700
Secondary accession number(s): D6VXR0
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1990
Last sequence update: April 1, 1990
Last modified: July 18, 2018
This is version 177 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal 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
  3. Yeast
    Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
  4. Yeast chromosome XI
    Yeast (Saccharomyces cerevisiae) chromosome XI: entries and gene names

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