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Protein

Uridylate kinase

Gene

pyrH

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor. Is also able to phosphorylate dUMP, although much less efficiently.1 Publication

Catalytic activityi

ATP + UMP = ADP + UDP.

Enzyme regulationi

Unlike most bacteria, is not activated by GTP. UTP acts as a competitive inhibitor against both substrates. High concentration of UMP abolishes the inhibition of UTP at low ATP concentrations, indicating that UTP binds to the acceptor site (UMP site).1 Publication

Kineticsi

  1. KM=14 µM for UMP (at pH 7.2)1 Publication
  2. KM=81 µM for ATP (at pH 7.2)1 Publication
  1. Vmax=5 µmol/min/mg enzyme (at pH 5.5)1 Publication
  2. Vmax=45 µmol/min/mg enzyme (at pH 7.2)1 Publication
  3. Vmax=12 µmol/min/mg enzyme (at pH 8.5)1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Pathwayi: CTP biosynthesis via de novo pathway

This protein is involved in step 1 of the subpathway that synthesizes UDP from UMP (UMPK route).
Proteins known to be involved in this subpathway in this organism are:
  1. Uridylate kinase (pyrH)
This subpathway is part of the pathway CTP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes UDP from UMP (UMPK route), the pathway CTP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei44 – 441UMP; via amide nitrogen1 Publication
Binding sitei45 – 451ATP; via amide nitrogen
Binding sitei49 – 491ATP
Binding sitei66 – 661UMP1 Publication
Binding sitei140 – 1401ATP
Binding sitei141 – 1411ATP
Binding sitei146 – 1461ATP; via amide nitrogen and carbonyl oxygen
Binding sitei149 – 1491ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi7 – 115ATP
Nucleotide bindingi114 – 1207UMP1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSSOL273057:GCH2-929-MONOMER.
BRENDAi2.7.4.22. 6163.
UniPathwayiUPA00159; UER00275.

Names & Taxonomyi

Protein namesi
Recommended name:
Uridylate kinase (EC:2.7.4.22)
Short name:
UK
Alternative name(s):
Uridine monophosphate kinase
Short name:
UMP kinase
Short name:
UMPK
Gene namesi
Name:pyrH
Ordered Locus Names:SSO0976
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 227227Uridylate kinasePRO_0000143927Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi273057.SSO0976.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi3 – 86Combined sources
Helixi11 – 144Combined sources
Helixi18 – 3316Combined sources
Beta strandi37 – 426Combined sources
Helixi45 – 5713Combined sources
Helixi62 – 8423Combined sources
Helixi96 – 1038Combined sources
Beta strandi106 – 1116Combined sources
Helixi120 – 13011Combined sources
Beta strandi134 – 14411Combined sources
Beta strandi146 – 1483Combined sources
Turni150 – 1523Combined sources
Beta strandi153 – 1553Combined sources
Beta strandi160 – 1634Combined sources
Helixi164 – 1718Combined sources
Turni179 – 1813Combined sources
Helixi187 – 1959Combined sources
Beta strandi199 – 2046Combined sources
Helixi205 – 2106Combined sources
Helixi211 – 2155Combined sources
Beta strandi222 – 2254Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J4JX-ray2.10A/B/C/D/E/F2-227[»]
2J4KX-ray2.20A/B/C/D/E/F2-227[»]
2J4LX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L2-227[»]
ProteinModelPortaliQ97ZE2.
SMRiQ97ZE2. Positions 2-227.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ97ZE2.

Family & Domainsi

Sequence similaritiesi

Belongs to the UMP kinase family.Curated

Phylogenomic databases

eggNOGiarCOG00858. Archaea.
COG0528. LUCA.
HOGENOMiHOG000047188.
InParanoidiQ97ZE2.
KOiK09903.
OMAiIRVIVMN.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_01220_A. PyrH_A.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR011818. Uridylate_kinase_arch/spir.
[Graphical view]
PANTHERiPTHR21499:SF23. PTHR21499:SF23. 1 hit.
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR02076. pyrH_arch. 1 hit.

Sequencei

Sequence statusi: Complete.

Q97ZE2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMNIILKISG KFFDEDNVDN LIVLRQSIKE LADNGFRVGI VTGGGSTARR
60 70 80 90 100
YIKLAREIGI GEAYLDLLGI WASRLNAYLV MFSLQDLAYM HVPQSLEEFI
110 120 130 140 150
QDWSHGKVVV TGGFQPGQST AAVAALVAEA SSSKTLVVAT NVDGVYEKDP
160 170 180 190 200
RIYADVKLIP HLTTQDLRKI LEGSQSVQAG TYELLDPLAI KIVERSKIRV
210 220
IVMNYRKLNR IIDILKGEEV SSIIEPV
Length:227
Mass (Da):25,120
Last modified:October 1, 2001 - v1
Checksum:i25FB40F5D19B34F2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK41250.1.
PIRiC90249.

Genome annotation databases

EnsemblBacteriaiAAK41250; AAK41250; SSO0976.
KEGGisso:SSO0976.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK41250.1.
PIRiC90249.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2J4JX-ray2.10A/B/C/D/E/F2-227[»]
2J4KX-ray2.20A/B/C/D/E/F2-227[»]
2J4LX-ray2.80A/B/C/D/E/F/G/H/I/J/K/L2-227[»]
ProteinModelPortaliQ97ZE2.
SMRiQ97ZE2. Positions 2-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0976.

Protocols and materials databases

DNASUi1455217.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK41250; AAK41250; SSO0976.
KEGGisso:SSO0976.

Phylogenomic databases

eggNOGiarCOG00858. Archaea.
COG0528. LUCA.
HOGENOMiHOG000047188.
InParanoidiQ97ZE2.
KOiK09903.
OMAiIRVIVMN.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00275.
BioCyciSSOL273057:GCH2-929-MONOMER.
BRENDAi2.7.4.22. 6163.

Miscellaneous databases

EvolutionaryTraceiQ97ZE2.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_01220_A. PyrH_A.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR011818. Uridylate_kinase_arch/spir.
[Graphical view]
PANTHERiPTHR21499:SF23. PTHR21499:SF23. 1 hit.
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR02076. pyrH_arch. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.
  2. "Structural and enzymatic investigation of the Sulfolobus solfataricus uridylate kinase shows competitive UTP inhibition and the lack of GTP stimulation."
    Jensen K.S., Johansson E., Jensen K.F.
    Biochemistry 46:2745-2757(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-227 IN COMPLEX WITH UMP; ATP ANALOG AND UTP, FUNCTION, ENZYME REGULATION, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.
    Strain: ATCC 35092 / DSM 1617 / JCM 11322 / P2.

Entry informationi

Entry nameiPYRH_SULSO
AccessioniPrimary (citable) accession number: Q97ZE2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 30, 2002
Last sequence update: October 1, 2001
Last modified: November 11, 2015
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Catalysis proceeds by a sequential bi-bi reaction mechanism of random order.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

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

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 one 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.