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A9M3K6 (UPP_NEIM0) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 41. 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:
Uracil phosphoribosyltransferase

EC=2.4.2.9
Alternative name(s):
UMP pyrophosphorylase
UPRTase
Gene names
Name:upp
Ordered Locus Names:NMCC_0738
OrganismNeisseria meningitidis serogroup C (strain 053442) [Complete proteome] [HAMAP]
Taxonomic identifier374833 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNeisserialesNeisseriaceaeNeisseria

Protein attributes

Sequence length208 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of uracil and 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to UMP and diphosphate By similarity. HAMAP-Rule MF_01218

Catalytic activity

UMP + diphosphate = uracil + 5-phospho-alpha-D-ribose 1-diphosphate. HAMAP-Rule MF_01218

Cofactor

Binds 1 Mg2+ ion per subunit. The magnesium is bound as Mg-PRPP By similarity.

Enzyme regulation

Allosterically activated by GTP By similarity. HAMAP-Rule MF_01218

Pathway

Pyrimidine metabolism; UMP biosynthesis via salvage pathway; UMP from uracil: step 1/1. HAMAP-Rule MF_01218

Sequence similarities

Belongs to the UPRTase family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 208208Uracil phosphoribosyltransferase HAMAP-Rule MF_01218
PRO_1000085630

Regions

Region130 – 13895-phospho-alpha-D-ribose 1-diphosphate binding By similarity
Region198 – 2003Uracil binding By similarity

Sites

Binding site7815-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site10315-phospho-alpha-D-ribose 1-diphosphate By similarity
Binding site1931Uracil; via amide nitrogen By similarity
Binding site19915-phospho-alpha-D-ribose 1-diphosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
A9M3K6 [UniParc].

Last modified February 5, 2008. Version 1.
Checksum: 7C1E6F6601200D04

FASTA20822,740
        10         20         30         40         50         60 
MNVNVINHPL VRHKLTLMRE ADCSTYKFRT LAIELARLMA YEASRDFEIE KYLIDGWCGQ 

        70         80         90        100        110        120 
IEGDRIKGKT LTVVPILRAG LGMLDGVLDL IPTAKISVVG LQRDEETLKP VSYFEKFVDS 

       130        140        150        160        170        180 
MDERPALIID PMLATGGSMV ATIDLLKAKG CKNIKALVLV AAPEGVKAVN DAHPDVTIYT 

       190        200 
AALDSHLNEN GYIIPGLGDA GDKIFGTR 

« Hide

References

[1]"Characterization of ST-4821 complex, a unique Neisseria meningitidis clone."
Peng J., Yang L., Yang F., Yang J., Yan Y., Nie H., Zhang X., Xiong Z., Jiang Y., Cheng F., Xu X., Chen S., Sun L., Li W., Shen Y., Shao Z., Liang X., Xu J., Jin Q.
Genomics 91:78-87(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 053442.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000381 Genomic DNA. Translation: ABX72931.1.
RefSeqYP_001598885.1. NC_010120.1.

3D structure databases

ProteinModelPortalA9M3K6.
SMRA9M3K6. Positions 6-208.
ModBaseSearch...

Protein-protein interaction databases

STRING374833.NMCC_0738.

Proteomic databases

PRIDEA9M3K6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABX72931; ABX72931; NMCC_0738.
GeneID5796403.
KEGGnmn:NMCC_0738.
PATRIC20345921. VBINeiMen117761_0883.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0035.
HOGENOMHOG000262754.
KOK00761.
OMATIEGWCG.
ProtClustDBPRK00129.

Enzyme and pathway databases

BioCycNMEN374833:GJ7Z-736-MONOMER.
UniPathwayUPA00574; UER00636.

Family and domain databases

HAMAPMF_01218_B. Upp_B.
InterProIPR000836. PRibTrfase_dom.
IPR005765. Ura_phspho_trans.
[Graphical view]
PfamPF00156. Pribosyltran. 1 hit.
[Graphical view]
TIGRFAMsTIGR01091. upp. 1 hit.
ProtoNetSearch...

Entry information

Entry nameUPP_NEIM0
AccessionPrimary (citable) accession number: A9M3K6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: February 5, 2008
Last modified: May 1, 2013
This is version 41 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