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P43890 (PYRH_HAEIN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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
Synonyms:smbA
Ordered Locus Names:HI_1065
OrganismHaemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd)
Taxonomic identifier71421 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the reversible phosphorylation of UMP to UDP. Ref.2

Catalytic activity

ATP + UMP = ADP + UDP. HAMAP MF_01220_B

Enzyme regulation

Allosterically activated by GTP. Inhibited by UTP. Ref.2

Pathway

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

Subunit structure

Homohexamer. Ref.2

Subcellular location

Cytoplasm By similarity HAMAP MF_01220_B.

Sequence similarities

Belongs to the UMP kinase family.

Biophysicochemical properties

Kinetic parameters:

KM=1.57 mM for ATP (in the absence of GTP) Ref.2

KM=0.46 mM for ATP (in the presence of GTP)

KM=40 µM for UMP

Vmax=57 µmol/min/mg enzyme

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandATP-binding
Nucleotide-binding
   Molecular functionKinase
Transferase
   Technical term3D-structure
Allosteric enzyme
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological processcellular amino acid biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   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 – 237237Uridylate kinase HAMAP MF_01220_B
PRO_0000143847

Regions

Nucleotide binding12 – 154ATP By similarity
Nucleotide binding135 – 1428UMP By similarity
Region20 – 256Involved in allosteric activation by GTP Potential

Sites

Binding site541UMP; via amide nitrogen By similarity
Binding site551ATP; via amide nitrogen By similarity
Binding site591ATP By similarity
Binding site741UMP By similarity
Binding site1621ATP By similarity
Binding site1681ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1711ATP By similarity

Secondary structure

1 ........................................... 237
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P43890 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: FDB0D6CE2CBCDCE3

FASTA23725,726
        10         20         30         40         50         60 
MSQPIYKRIL LKLSGEALQG EDGLGIDPAI LDRMAVEIKE LVEMGVEVSV VLGGGNLFRG 

        70         80         90        100        110        120 
AKLAKAGMNR VVGDHMGMLA TVMNGLAMRD SLFRADVNAK LMSAFQLNGI CDTYNWSEAI 

       130        140        150        160        170        180 
KMLREKRVVI FSAGTGNPFF TTDSTACLRG IEIEADVVLK ATKVDGVYDC DPAKNPDAKL 

       190        200        210        220        230 
YKNLSYAEVI DKELKVMDLS AFTLARDHGM PIRVFNMGKP GALRQVVTGT EEGTTIC

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
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: 17210578] [Abstract]
Cited for: FUNCTION, ENZYME REGULATION, KINETIC PARAMETERS, 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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		L42023 Genomic DNA. Translation: AAC22719.1.
PIRH64180.
RefSeqNP_439223.1. NC_000907.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2A1FX-ray2.10A/B/C/D/E/F2-237[»]
ProteinModelPortalP43890.
SMRP43890. Positions 2-237.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID950042.
GenomeReviewsGene locus HI_1065 in contig L42023_GR.
KEGGhin:HI1065.
NMPDRfig|71421.1.peg.1024.
PATRIC20190793. VBIHaeInf48452_1109.
TIGRHI_1065.

Phylogenomic databases

HOGENOMHBG497552.
OMARHMEKGR.
PhylomeDBP43890.
ProtClustDBPRK00358.

Enzyme and pathway databases

BioCycHINF71421:HI_1065-MONOMER.

Family and domain databases

HAMAPMF_01220_B. PyrH_B.
[Tree]
InterProIPR001048. Asp/Glu/Uridylate_kinase.
IPR011817. Uridylate_kinase.
IPR015963. Uridylate_kinase_bac.
[Graphical view]
Gene3DG3DSA:3.40.1160.10. Aa_kinase. 1 hit.
KOK09903.
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_HAEIN
AccessionPrimary (citable) accession number: P43890
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: January 25, 2012
This is version 79 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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