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Reviewed, UniProtKB/Swiss-Prot Q9PJ84 (PYRG_CAMJE)

Last modified June 16, 2009. Version 49. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    CTP synthase
    EC=6.3.4.2
Alternative name(s):
    UTP--ammonia ligase
    CTP synthetase
Gene names
Name: pyrG
Ordered Locus Names: Cj0027
OrganismCampylobacter jejuni [Complete proteome] [HAMAP]
Taxonomic identifier197 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter

Protein attributes

Sequence length543 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen By similarity.

Catalytic activity

ATP + UTP + NH3 = ADP + phosphate + CTP. HAMAP MF_01227

Enzyme regulation

Allosterically activated by GTP, when glutamine is the substrate. Inhibited by CTP By similarity.

Pathway

Pyrimidine metabolism; CTP biosynthesis via de novo pathway; CTP from UDP: step 2/2. HAMAP MF_01227

Subunit structure

Homotetramer By similarity.

Sequence similarities

Belongs to the CTP synthase family.

Contains 1 glutamine amidotransferase type-1 domain.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 543543CTP synthase HAMAP MF_01227
PRO_0000138172

Regions

Domain292 – 543252Glutamine amidotransferase type-1
Region1 – 254254Aminator domain HAMAP MF_01227

Sites

Active site3811Nucleophile By similarity
Active site5161 By similarity
Active site5181 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9PJ84-1 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: 5DA89FA7D4C680EA

FASTA54360,401
        10         20         30         40         50         60 
MKQTKYIFVT GGVLSSLGKG IAAASIATLL KNSGLKVSIL KADPYINVDP GTMSPFEHGE 

        70         80         90        100        110        120 
VFVTDDGAET DLDLGHYERF LDESLSQDNN FTTGRVYQSV IEKERRGEYL GKTIQVIPHI 

       130        140        150        160        170        180 
VGEIKDRIKK AGEGKDILIV EIGGTVGDIE GLPFLEAIRA LRLEVGKNNA MNIHLTLVPF 

       190        200        210        220        230        240 
IKAAGELKTK PTQHSVGELR RIGISPDMII CRSEKALDRD LKDKIAISCG VEKNCVIESV 

       250        260        270        280        290        300 
DAASIYQIPL NFLKQDILSP IAEILDLKNL KPNMENWDSL VKRVIAPSNE VKIAFVGKYV 

       310        320        330        340        350        360 
DLKESYKSLT EAIIHAGAAL DTKVELKWVD SEKLENMESS EVFKDVSGIL VAGGFGYRGV 

       370        380        390        400        410        420 
EGKIKAIQYA RENKIPFLGI CLGMQLALVE FARNVLKLKD VNSSEFNEKC QNPVVYLIDE 

       430        440        450        460        470        480 
FMDTNGEKQI RTAKTPLGGT MRLGAYKCDI KEKSLLAKVY NEVKSVKERH RHRYEANPKY 

       490        500        510        520        530        540 
RADFEKYGLI VSGESKGLIE AVELNCHPFF LAVQFHPEFT SRLEHVNPVI CSFIKAAINY 


EDN 

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References

[1]"The genome sequence of the food-borne pathogen Campylobacter jejuni reveals hypervariable sequences."
Parkhill J., Wren B.W., Mungall K.L., Ketley J.M., Churcher C.M., Basham D., Chillingworth T., Davies R.M., Feltwell T., Holroyd S., Jagels K., Karlyshev A.V., Moule S., Pallen M.J., Penn C.W., Quail M.A., Rajandream M.A., Rutherford K.M. expand/collapse author list , van Vliet A.H.M., Whitehead S., Barrell B.G.
Nature 403:665-668(2000) [PubMed: 10688204] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NCTC 11168 / Serotype O:2.

Cross-references

Sequence databases

AL111168 Genomic DNA. Translation: CAL34208.1.
PIRF81418.
RefSeqYP_002343499.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActQ9PJ84. 49 interactions.

Genome annotation databases

GeneID904367.
GenomeReviewsGene locus Cj0027 in contig AL111168_GR.
KEGGcje:Cj0027.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAQ9PJ84. CESKSHI.

Enzyme and pathway databases

BioCycCJEJ192222:CJ0027-MON.
BRENDA6.3.4.2. 255835.

Family and domain databases

HAMAPMF_01227.
[Tree]
InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE_1.
IPR000991. GATase_class1_C.
[Graphical view]
PANTHERPTHR11550. PyrG_synth. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRG_CAMJE
AccessionPrimary (citable) accession number: Q9PJ84
Secondary accession number(s): Q0PC98
Entry history
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2000
Last modified: June 16, 2009
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents