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Protein

Uridylate kinase

Gene

pyrH

Organism
Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the reversible phosphorylation of UMP to UDP.1 Publication

Catalytic activityi

ATP + UMP = ADP + UDP.

Enzyme regulationi

Allosterically activated by GTP. Inhibited by UTP.1 Publication

Kineticsi

  1. KM=1.57 mM for ATP (in the absence of GTP)1 Publication
  2. KM=0.46 mM for ATP (in the presence of GTP)1 Publication
  3. KM=40 µM for UMP1 Publication
  1. Vmax=57 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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541UMP; via amide nitrogenBy similarity
Binding sitei55 – 551ATP; via amide nitrogenBy similarity
Binding sitei59 – 591ATPBy similarity
Binding sitei74 – 741UMPBy similarity
Binding sitei162 – 1621ATPBy similarity
Binding sitei168 – 1681ATP; via amide nitrogen and carbonyl oxygenBy similarity
Binding sitei171 – 1711ATPBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi12 – 154ATPBy similarity
Nucleotide bindingi135 – 1428UMPBy similarity

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

SABIO-RKP43890.
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:HI_1065
OrganismiHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifieri71421 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus
Proteomesi
  • UP000000579 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 – 237237Uridylate kinasePRO_0000143847Add
BLAST

Interactioni

Subunit structurei

Homohexamer.1 Publication

Protein-protein interaction databases

STRINGi71421.HI1065.

Structurei

Secondary structure

1
237
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 137Combined sources
Helixi15 – 184Combined sources
Beta strandi23 – 253Combined sources
Helixi28 – 4215Combined sources
Turni43 – 453Combined sources
Beta strandi47 – 526Combined sources
Turni55 – 573Combined sources
Helixi61 – 655Combined sources
Helixi70 – 9425Combined sources
Beta strandi99 – 1057Combined sources
Turni108 – 1103Combined sources
Beta strandi111 – 1133Combined sources
Helixi116 – 1249Combined sources
Beta strandi128 – 1336Combined sources
Helixi142 – 15211Combined sources
Beta strandi156 – 16611Combined sources
Beta strandi182 – 1843Combined sources
Helixi186 – 1916Combined sources
Helixi199 – 20810Combined sources
Beta strandi212 – 2165Combined sources
Helixi222 – 2276Combined sources
Beta strandi232 – 2365Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A1FX-ray2.10A/B/C/D/E/F2-237[»]
ProteinModelPortaliP43890.
SMRiP43890. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43890.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni20 – 256Involved in allosteric activation by GTPSequence analysis

Sequence similaritiesi

Belongs to the UMP kinase family.Curated

Phylogenomic databases

eggNOGiENOG4105C41. Bacteria.
COG0528. LUCA.
KOiK09903.
OMAiIIVFDMN.
OrthoDBiEOG6M0T8S.
PhylomeDBiP43890.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_01220_B. PyrH_B.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR015963. Uridylate_kinase_bac.
[Graphical view]
PANTHERiPTHR21499:SF23. PTHR21499:SF23. 1 hit.
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR02075. pyrH_bact. 1 hit.

Sequencei

Sequence statusi: Complete.

P43890-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQPIYKRIL LKLSGEALQG EDGLGIDPAI LDRMAVEIKE LVEMGVEVSV
60 70 80 90 100
VLGGGNLFRG AKLAKAGMNR VVGDHMGMLA TVMNGLAMRD SLFRADVNAK
110 120 130 140 150
LMSAFQLNGI CDTYNWSEAI KMLREKRVVI FSAGTGNPFF TTDSTACLRG
160 170 180 190 200
IEIEADVVLK ATKVDGVYDC DPAKNPDAKL YKNLSYAEVI DKELKVMDLS
210 220 230
AFTLARDHGM PIRVFNMGKP GALRQVVTGT EEGTTIC
Length:237
Mass (Da):25,726
Last modified:November 1, 1995 - v1
Checksum:iFDB0D6CE2CBCDCE3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22719.1.
PIRiH64180.
RefSeqiNP_439223.1. NC_000907.1.
WP_005693391.1. NC_000907.1.

Genome annotation databases

EnsemblBacteriaiAAC22719; AAC22719; HI_1065.
GeneIDi950042.
KEGGihin:HI1065.
PATRICi20190793. VBIHaeInf48452_1109.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L42023 Genomic DNA. Translation: AAC22719.1.
PIRiH64180.
RefSeqiNP_439223.1. NC_000907.1.
WP_005693391.1. NC_000907.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2A1FX-ray2.10A/B/C/D/E/F2-237[»]
ProteinModelPortaliP43890.
SMRiP43890. Positions 2-237.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi71421.HI1065.

Protocols and materials databases

DNASUi950042.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC22719; AAC22719; HI_1065.
GeneIDi950042.
KEGGihin:HI1065.
PATRICi20190793. VBIHaeInf48452_1109.

Phylogenomic databases

eggNOGiENOG4105C41. Bacteria.
COG0528. LUCA.
KOiK09903.
OMAiIIVFDMN.
OrthoDBiEOG6M0T8S.
PhylomeDBiP43890.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00275.
SABIO-RKP43890.

Miscellaneous databases

EvolutionaryTraceiP43890.

Family and domain databases

Gene3Di3.40.1160.10. 1 hit.
HAMAPiMF_01220_B. PyrH_B.
InterProiIPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR015963. Uridylate_kinase_bac.
[Graphical view]
PANTHERiPTHR21499:SF23. PTHR21499:SF23. 1 hit.
PfamiPF00696. AA_kinase. 1 hit.
[Graphical view]
PIRSFiPIRSF005650. Uridylate_kin. 1 hit.
SUPFAMiSSF53633. SSF53633. 1 hit.
TIGRFAMsiTIGR02075. pyrH_bact. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
  2. "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: FUNCTION, ENZYME REGULATION, KINETIC PARAMETERS, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT.
  3. "Crystal structure of uridylate kinase."
    New York structural genomics research consortium (NYSGRC)
    Submitted (JUN-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 2-237.

Entry informationi

Entry nameiPYRH_HAEIN
AccessioniPrimary (citable) accession number: P43890
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 11, 2015
This is version 109 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Allosteric enzyme, Complete proteome, Reference proteome

Documents

  1. Haemophilus influenzae
    Haemophilus influenzae (strain Rd): entries and gene names
  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

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.