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P74457 (PYRH_SYNY3) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·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
Ordered Locus Names:sll0144
OrganismSynechocystis sp. (strain PCC 6803 / Kazusa)
Taxonomic identifier1111708 [NCBI]
Taxonomic lineageBacteriaCyanobacteriaChroococcalesSynechocystis

Protein attributes

Sequence length260 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the reversible phosphorylation of UMP to UDP By similarity. HAMAP MF_01220_B

Catalytic activity

ATP + UMP = ADP + UDP. HAMAP MF_01220_B

Enzyme regulation

Allosterically activated by GTP. Inhibited by UTP By similarity. HAMAP MF_01220_B

Pathway

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

Subunit structure

Homohexamer By similarity. HAMAP MF_01220_B

Subcellular location

Cytoplasm By similarity HAMAP MF_01220_B.

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
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 – 260260Uridylate kinase HAMAP MF_01220_B
PRO_0000143898

Regions

Nucleotide binding29 – 324ATP By similarity
Nucleotide binding152 – 1598UMP By similarity
Region37 – 426Involved in allosteric activation by GTP Potential

Sites

Binding site711UMP; via amide nitrogen By similarity
Binding site721ATP; via amide nitrogen By similarity
Binding site761ATP By similarity
Binding site911UMP By similarity
Binding site1791ATP By similarity
Binding site1851ATP; via amide nitrogen and carbonyl oxygen By similarity
Binding site1881ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
P74457 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: E234C011E3CB4C98

FASTA26027,651
        10         20         30         40         50         60 
MGGILRLTLI PCLYINGDGG MSYQRVLLKL SGEALMGDLG YGIDPAVVGT IAQEIKDVLQ 

        70         80         90        100        110        120 
AGVQLAIVVG GGNIFRGVKA SAAGMDRATA DYIGMIATVM NAMTLQDALE QMDIPTRVLT 

       130        140        150        160        170        180 
AIAMQEVAEP YIRRRAIRHL EKGRVVIFGA GSGNPFFTTD TTAALRAAEI DAEVVFKATK 

       190        200        210        220        230        240 
VDGVYDSDPK TNPNARRFTT LTYSHVLAED LKVMDSTAIA LCKDNNIPIM IFDLGVPGNI 

       250        260 
VRAIKGEAVG TLVGENCEVS 

« Hide

References

[1]"Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions."
Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S. expand/collapse author list , Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.
DNA Res. 3:109-136(1996) [PubMed: 8905231] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27184 / PCC 6803 / N-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000022 Genomic DNA. Translation: BAA18558.1.
PIRS76429.

3D structure databases

ProteinModelPortalP74457.
SMRP74457. Positions 21-253.
ModBaseSearch...

Protein-protein interaction databases

IntActP74457. 3 interactions.
STRINGP74457.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GenomeReviewsGene locus sll0144 in contig BA000022_GR.
KEGGsyn:sll0144.
NMPDRfig|1148.1.peg.1981.

Phylogenomic databases

eggNOGCOG0528.
HOGENOMHBG497552.
OMARHMEKGR.
PhylomeDBP74457.
ProtClustDBPRK00358.

Enzyme and pathway databases

BioCycSSP1148:SLL0144-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_SYNY3
AccessionPrimary (citable) accession number: P74457
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: February 1, 1997
Last modified: January 25, 2012
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Synechocystis PCC 6803

Synechocystis (strain PCC 6803): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families