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Protein

Uridylate kinase

Gene

pyrH

Organism
Escherichia coli (strain K12)
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.1 Publication

Miscellaneous

The peripheral distribution of PyrH is related most probably to its role in the synthesis of membrane sugar components.

Catalytic activityi

ATP + UMP = ADP + UDP.

Enzyme regulationi

Allosterically activated by GTP. Competitively inhibited by magnesium-free UTP. Magnesium-bound UTP is unable to inhibit enzyme activity.2 Publications

Kineticsi

  1. KM=120 µM for ATP1 Publication
  2. KM=50 µM for UMP1 Publication
  1. Vmax=96 µmol/min/mg enzyme1 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)DescriptionActionsGraphical viewLength
Binding sitei57UMP; via amide nitrogen1 Publication1
Binding sitei58ATP; via amide nitrogenBy similarity1
Binding sitei62ATPBy similarity1
Binding sitei77UMP1 Publication1
Binding sitei165ATPBy similarity1
Binding sitei171ATP; via amide nitrogen and carbonyl oxygenBy similarity1
Binding sitei174ATPBy similarity1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 18ATPBy similarity4
Nucleotide bindingi138 – 145UMP1 Publication8

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • identical protein binding Source: EcoCyc
  • UMP kinase activity Source: EcoCyc

GO - Biological processi

  • 'de novo' CTP biosynthetic process Source: UniProtKB-UniPathway
  • pyrimidine nucleotide biosynthetic process Source: EcoCyc

Keywordsi

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

Enzyme and pathway databases

BioCyciEcoCyc:UMPKI-MONOMER.
MetaCyc:UMPKI-MONOMER.
BRENDAi2.7.4.22. 2026.
SABIO-RKiP0A7E9.
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
Synonyms:smbA
Ordered Locus Names:b0171, JW0166
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG11539. pyrH.

Subcellular locationi

P0A7E9:

GO - Cellular componenti

  • cytosol Source: EcoCyc

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi62R → H: Loss of activation by GTP and decreased affinity for UTP. 1 Publication1
Mutagenesisi77D → N: Loss of activation by GTP and decreased affinity for UTP. 1 Publication1
Mutagenesisi138T → A: Loss of activation by GTP. Moderate loss of sensitivity to UTP inhibition. 4-fold and 2-fold decrease in affinity for UMP and ATP, respectively. 1 Publication1
Mutagenesisi140N → A: Loss of activation by GTP. Moderate loss of sensitivity to UTP inhibition. 1 Publication1
Mutagenesisi146D → N: Drastically reduced activity. 1 Publication1
Mutagenesisi159D → N: Increased solubility at neutral pH. Nearly no change in kinetic properties and stability. 1 Publication1
Mutagenesisi174D → N: Reduced UMP-binding affinity. 1 Publication1
Mutagenesisi201D → N: Loss of activation by GTP. 2 Publications1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemoved1 Publication
ChainiPRO_00001438422 – 241Uridylate kinaseAdd BLAST240

Proteomic databases

PaxDbiP0A7E9.
PRIDEiP0A7E9.

Interactioni

Subunit structurei

Homohexamer.2 Publications

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

BioGridi4262225. 6 interactors.
DIPiDIP-31830N.
IntActiP0A7E9. 54 interactors.
MINTiMINT-1222953.
STRINGi316385.ECDH10B_0151.

Structurei

Secondary structure

1241
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi10 – 16Combined sources7
Helixi18 – 21Combined sources4
Beta strandi26 – 28Combined sources3
Helixi31 – 46Combined sources16
Beta strandi50 – 55Combined sources6
Turni58 – 60Combined sources3
Helixi63 – 68Combined sources6
Helixi73 – 97Combined sources25
Beta strandi102 – 108Combined sources7
Turni111 – 113Combined sources3
Beta strandi114 – 116Combined sources3
Helixi119 – 127Combined sources9
Beta strandi131 – 136Combined sources6
Beta strandi139 – 142Combined sources4
Helixi145 – 155Combined sources11
Beta strandi159 – 169Combined sources11
Beta strandi171 – 173Combined sources3
Turni175 – 177Combined sources3
Beta strandi185 – 188Combined sources4
Helixi189 – 194Combined sources6
Helixi202 – 210Combined sources9
Beta strandi215 – 219Combined sources5
Helixi225 – 230Combined sources6
Beta strandi236 – 240Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2BNDX-ray2.60A/B1-241[»]
2BNEX-ray2.30A/B1-241[»]
2BNFX-ray2.45A/B1-241[»]
2V4YX-ray2.80A/B/C/D/E/F1-241[»]
ProteinModelPortaliP0A7E9.
SMRiP0A7E9.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7E9.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni23 – 28Involved in allosteric activation by GTPSequence analysis6

Sequence similaritiesi

Belongs to the UMP kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105C41. Bacteria.
COG0528. LUCA.
HOGENOMiHOG000047187.
InParanoidiP0A7E9.
KOiK09903.
PhylomeDBiP0A7E9.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_01220_B. PyrH_B. 1 hit.
InterProiView protein in InterPro
IPR036393. AceGlu_kinase-like_sf.
IPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR015963. Uridylate_kinase_bac.
PfamiView protein in Pfam
PF00696. AA_kinase. 1 hit.
PIRSFiPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR02075. pyrH_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

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

P0A7E9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MATNAKPVYK RILLKLSGEA LQGTEGFGID ASILDRMAQE IKELVELGIQ
60 70 80 90 100
VGVVIGGGNL FRGAGLAKAG MNRVVGDHMG MLATVMNGLA MRDALHRAYV
110 120 130 140 150
NARLMSAIPL NGVCDSYSWA EAISLLRNNR VVILSAGTGN PFFTTDSAAC
160 170 180 190 200
LRGIEIEADV VLKATKVDGV FTADPAKDPT ATMYEQLTYS EVLEKELKVM
210 220 230 240
DLAAFTLARD HKLPIRVFNM NKPGALRRVV MGEKEGTLIT E
Length:241
Mass (Da):25,970
Last modified:January 23, 2007 - v2
Checksum:i82EFA75F7226E201
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti64 – 69AGLAKA → RWSGET in CAA55388 (Ref. 1) Curated6

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti62R → H in Smba9. 1
Natural varianti201D → N in Smba2. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78809 Genomic DNA. Translation: CAA55388.1.
D13334 Genomic DNA. Translation: BAA02598.1.
U70214 Genomic DNA. Translation: AAB08600.1.
U00096 Genomic DNA. Translation: AAC73282.1.
AP009048 Genomic DNA. Translation: BAB96747.1.
PIRiB45269.
RefSeqiNP_414713.1. NC_000913.3.
WP_000224573.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC73282; AAC73282; b0171.
BAB96747; BAB96747; BAB96747.
GeneIDi944989.
KEGGiecj:JW0166.
eco:b0171.
PATRICifig|1411691.4.peg.2109.

Similar proteinsi

Entry informationi

Entry nameiPYRH_ECOLI
AccessioniPrimary (citable) accession number: P0A7E9
Secondary accession number(s): P29464
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: October 25, 2017
This is version 110 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families