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Q0TLG2 (PYRH_ECOL5) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 52. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Uridylate kinase
Short name=UK
EC=2.7.4.22
Alternative name(s):
Uridine monophosphate kinase
Short name=UMP kinase
Short name=UMPK
Gene names
Name:pyrH
Ordered Locus Names:ECP_0179
OrganismEscherichia coli O6:K15:H31 (strain 536 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier362663 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia ›

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible phosphorylation of UMP to UDP By similarity. HAMAP-Rule MF_01220

Catalytic activity

ATP + UMP = ADP + UDP. HAMAP-Rule MF_01220

Enzyme regulation

Allosterically activated by GTP. Inhibited by UTP By similarity. HAMAP-Rule MF_01220

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1. HAMAP-Rule MF_01220

Subunit structure

Homohexamer By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the UMP kinase family.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical termAllosteric enzyme
Complete proteome
Gene Ontology (GO)
   Biological_process'de novo' CTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

cellular amino acid biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

UMP kinase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 241241Uridylate kinase HAMAP-Rule MF_01220
PRO_1000053922

Regions

Nucleotide binding15 – 184ATP By similarity
Nucleotide binding138 – 1458UMP By similarity
Region23 – 286Involved in allosteric activation by GTP Potential

Sites

Binding site571UMP; via amide nitrogen By similarity
Binding site581ATP; via amide nitrogen By similarity
Binding site621ATP By similarity
Binding site771UMP By similarity
Binding site1651ATP By similarity
Binding site1711ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1741ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0TLG2 [UniParc].

Last modified September 5, 2006. Version 1.
Checksum: 82EFA75F7226E201

FASTA24125,970
        10         20         30         40         50         60 
MATNAKPVYK RILLKLSGEA LQGTEGFGID ASILDRMAQE IKELVELGIQ VGVVIGGGNL 

        70         80         90        100        110        120 
FRGAGLAKAG MNRVVGDHMG MLATVMNGLA MRDALHRAYV NARLMSAIPL NGVCDSYSWA 

       130        140        150        160        170        180 
EAISLLRNNR VVILSAGTGN PFFTTDSAAC LRGIEIEADV VLKATKVDGV FTADPAKDPT 

       190        200        210        220        230        240 
ATMYEQLTYS EVLEKELKVM DLAAFTLARD HKLPIRVFNM NKPGALRRVV MGEKEGTLIT 


E

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References

[1]"Role of pathogenicity island-associated integrases in the genome plasticity of uropathogenic Escherichia coli strain 536."
Hochhut B., Wilde C., Balling G., Middendorf B., Dobrindt U., Brzuszkiewicz E., Gottschalk G., Carniel E., Hacker J.
Mol. Microbiol. 61:584-595(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 536 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000247 Genomic DNA. Translation: ABG68219.1.
RefSeqYP_668118.1. NC_008253.1.

3D structure databases

ProteinModelPortalQ0TLG2.
SMRQ0TLG2. Positions 3-241.
ModBaseSearch...

Protein-protein interaction databases

STRING362663.ECP_0179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABG68219; ABG68219; ECP_0179.
GeneID4190261.
KEGGecp:ECP_0179.
PATRIC18190999. VBIEscCol77757_0183.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0528.
HOGENOMHOG000047187.
KOK09903.
OMARHMEKGR.
PhylomeDBQ0TLG2.
ProtClustDBPRK00358.

Enzyme and pathway databases

BioCycECOL362663:GIY5-177-MONOMER.
UniPathwayUPA00159; UER00275.

Family and domain databases

Gene3D3.40.1160.10. 1 hit.
HAMAPMF_01220_B. PyrH_B.
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR015963. Uridylate_kinase_bac.
[Graphical view]
PANTHERPTHR26059. PTHR26059. 1 hit.
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMSSF53633. Aa_kinase. 1 hit.
TIGRFAMsTIGR02075. pyrH_bact. 1 hit.
ProtoNetSearch...

Entry information

Entry namePYRH_ECOL5
AccessionPrimary (citable) accession number: Q0TLG2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 5, 2006
Last modified: May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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