Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

P0A7E9 (PYRH_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 86. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

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
Synonyms:smbA
Ordered Locus Names:b0171, JW0166
OrganismEscherichia coli (strain K12) [Reference proteome] [HAMAP]
Taxonomic identifier83333 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length241 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible phosphorylation of UMP to UDP, with ATP as the most efficient phosphate donor. Ref.3

Catalytic activity

ATP + UMP = ADP + UDP. HAMAP-Rule MF_01220_B

Enzyme regulation

Allosterically activated by GTP. Competitively inhibited by magnesium-free UTP. Magnesium-bound UTP is unable to inhibit enzyme activity. Ref.12 Ref.13

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; UDP from UMP (UMPK route): step 1/1. HAMAP-Rule MF_01220_B

Subunit structure

Homohexamer. Ref.3

Subcellular location

Cytoplasm. Note: Is predominantly localized near the bacterial membranes. Ref.10

Miscellaneous

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

Sequence similarities

Belongs to the UMP kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=120 µM for ATP Ref.3

KM=50 µM for UMP

Vmax=96 µmol/min/mg enzyme

Binary interactions

With

Entry

#Exp.

IntAct

Notes

deoDP0ABP81EBI-370182,EBI-907568

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.3
Chain2 – 241240Uridylate kinase HAMAP-Rule MF_01220_B
PRO_0000143842

Regions

Nucleotide binding15 – 184ATP By similarity
Nucleotide binding138 – 1458UMP HAMAP-Rule MF_01220_B
Region23 – 286Involved in allosteric activation by GTP Potential

Sites

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

Natural variations

Natural variant621R → H in Smba9.
Natural variant2011D → N in Smba2.

Experimental info

Mutagenesis621R → H: Loss of activation by GTP and decreased affinity for UTP. Ref.11
Mutagenesis771D → N: Loss of activation by GTP and decreased affinity for UTP. Ref.11
Mutagenesis1381T → 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. Ref.13
Mutagenesis1401N → A: Loss of activation by GTP. Moderate loss of sensitivity to UTP inhibition. Ref.13
Mutagenesis1461D → N: Drastically reduced activity. Ref.11
Mutagenesis1591D → N: Increased solubility at neutral pH. Nearly no change in kinetic properties and stability. Ref.11
Mutagenesis1741D → N: Reduced UMP-binding affinity. Ref.11
Mutagenesis2011D → N: Loss of activation by GTP. Ref.3 Ref.11
Sequence conflict64 – 696AGLAKA → RWSGET in CAA55388. Ref.1

Secondary structure

............................................... 241
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P0A7E9 [UniParc].

Last modified January 23, 2007. Version 2.
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 

« Hide

References

« Hide 'large scale' references
[1]"Cloning, nucleotide sequence and expression of the Escherichia coli K-12 pyrH gene encoding UMP kinase."
Smallshaw J.E., Kelln R.A.
Life Sci. Adv. (Genet.) 11:59-65(1992)
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], CHARACTERIZATION.
Strain: K12.
[2]"Identification and characterization of the smbA gene, a suppressor of the mukB null mutant of Escherichia coli."
Yamanaka K., Ogura T., Niki H., Hiraga S.
J. Bacteriol. 174:7517-7526(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]"Escherichia coli UMP-kinase, a member of the aspartokinase family, is a hexamer regulated by guanine nucleotides and UTP."
Serina L., Blondin C., Krin E., Sismeiro O., Danchin A., Sakamoto H., Gilles A.-M., Barzu O.
Biochemistry 34:5066-5074(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, CHARACTERIZATION, SUBUNIT, MUTAGENESIS OF ASP-201.
[4]"Systematic sequencing of the Escherichia coli genome: analysis of the 2.4-4.1 min (110,917-193,643 bp) region."
Fujita N., Mori H., Yura T., Ishihama A.
Nucleic Acids Res. 22:1637-1639(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]"Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region."
Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K.
Submitted (FEB-1996) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[6]"Sequence of minutes 4-25 of Escherichia coli."
Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M., Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D., Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.
Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[7]"The complete genome sequence of Escherichia coli K-12."
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y.
Science 277:1453-1462(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / MG1655 / ATCC 47076.
[8]"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[9]"Multicopy suppressors, mssA and mssB, of an smbA mutation of Escherichia coli."
Yamanaka K., Ogura T., Koonin E.V., Niki H., Hiraga S.
Mol. Gen. Genet. 243:9-16(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: CHARACTERIZATION.
[10]"Immunochemical analysis of UMP kinase from Escherichia coli."
Landais S., Gounon P., Laurent-Winter C., Mazie J.-C., Danchin A., Barzu O., Sakamoto H.
J. Bacteriol. 181:833-840(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
[11]"Mutational analysis of UMP kinase from Escherichia coli."
Bucurenci N., Serina L., Zaharia C., Landais S., Danchin A., Barzu O.
J. Bacteriol. 180:473-477(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: MUTAGENESIS OF ARG-62; ASP-77; ASP-146; ASP-159; ASP-174 AND ASP-201.
[12]"Regulatory mechanisms differ in UMP kinases from Gram-negative and Gram-positive bacteria."
Evrin C., Straut M., Slavova-Azmanova N., Bucurenci N., Onu A., Assairi L., Ionescu M., Palibroda N., Barzu O., Gilles A.-M.
J. Biol. Chem. 282:7242-7253(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: ENZYME REGULATION.
[13]"Structure of Escherichia coli UMP kinase differs from that of other nucleoside monophosphate kinases and sheds new light on enzyme regulation."
Briozzo P., Evrin C., Meyer P., Assairi L., Joly N., Barzu O., Gilles A.-M.
J. Biol. Chem. 280:25533-25540(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF MUTANT ASN-159 IN COMPLEX WITH UMP; UDP AND UTP, ENZYME REGULATION, MUTAGENESIS OF THR-138 AND ASN-140.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRB45269.
RefSeqNP_414713.1. NC_000913.3.
YP_488473.1. NC_007779.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP0A7E9.
SMRP0A7E9. Positions 3-241.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

DIPDIP-31830N.
IntActP0A7E9. 54 interactions.
MINTMINT-1222953.
STRING511145.b0171.

Proteomic databases

PaxDbP0A7E9.
PRIDEP0A7E9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC73282; AAC73282; b0171.
BAB96747; BAB96747; BAB96747.
GeneID12933231.
944989.
KEGGecj:Y75_p0167.
eco:b0171.
PATRIC32115451. VBIEscCol129921_0177.

Organism-specific databases

EchoBASEEB1501.
EcoGeneEG11539. pyrH.

Phylogenomic databases

eggNOGCOG0528.
HOGENOMHOG000047187.
KOK09903.
OMAASADYMG.
OrthoDBEOG6M0T8S.
PhylomeDBP0A7E9.
ProtClustDBPRK00358.

Enzyme and pathway databases

BioCycEcoCyc:UMPKI-MONOMER.
ECOL316407:JW0166-MONOMER.
MetaCyc:UMPKI-MONOMER.
BRENDA2.7.4.22. 2026.
SABIO-RKP0A7E9.
UniPathwayUPA00159; UER00275.

Gene expression databases

GenevestigatorP0A7E9.

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]
PfamPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMSSF53633. SSF53633. 1 hit.
TIGRFAMsTIGR02075. pyrH_bact. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP0A7E9.
PROP0A7E9.

Entry information

Entry namePYRH_ECOLI
AccessionPrimary (citable) accession number: P0A7E9
Secondary accession number(s): P29464
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 86 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene