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Reviewed, UniProtKB/Swiss-Prot Q1QZX9 (PYRG_CHRSD)

Last modified June 16, 2009. Version 27. 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 · 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: Csal_0617
OrganismChromohalobacter salexigens (strain DSM 3043 / ATCC BAA-138 / NCIMB 13768) [Complete proteome] [HAMAP]
Taxonomic identifier290398 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaOceanospirillalesHalomonadaceaeChromohalobacter

Protein attributes

Sequence length548 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 548548CTP synthase HAMAP MF_01227
PRO_0000266095

Regions

Domain290 – 541252Glutamine amidotransferase type-1
Region1 – 252252Aminator domain HAMAP MF_01227

Sites

Active site3781Nucleophile By similarity
Active site5141 By similarity
Active site5161 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QZX9-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: F765AC07F2405337

FASTA54860,663
        10         20         30         40         50         60 
MTRYIFVTGG VVSSLGKGIA SASLAAILEA RGLKVTILKL DPYINVDPGT MSPFQHGEVF 

        70         80         90        100        110        120 
VTEDGAETDL DLGHYERFIR TKMTQGNNFT TGRVYEHVLR KERRGDYLGG TVQVIPHITD 

       130        140        150        160        170        180 
EIKRRVYEGG DGFDVALVEI GGTVGDIESL PFLEATRQIR SEKGANQAIF MHLTLVPYIK 

       190        200        210        220        230        240 
TAGETKTKPT QHSVKELRSI GIQPDILICR SEVELEESER RKIALFTNVE ERAVVPLQDA 

       250        260        270        280        290        300 
DTIYRIPLML HEHGLDDIIC DKLRIEADEV DLAEWVRVLD AKLNPLKSVN IAMVGKYMEL 

       310        320        330        340        350        360 
LDAYKSLNEA LIHAGIQGRV KVNIDYIDSE DIEHHGTERL AGKDAILVPG GFGERGVEGK 

       370        380        390        400        410        420 
IATARYAREN GVPYLGICLG MQVAVIEYAR HVAGWADANS TEFTHDTQHP VVGLITEWVN 

       430        440        450        460        470        480 
AEGKIELRDA ASDLGGTMRL GGQVCHLKPG TRAHEAYGLD EITERHRHRF EVNNQFVEAL 

       490        500        510        520        530        540 
ESAGLVISGK SADHSLVEMI ELPEHPWYVA CQFHPEFTST PRDGHPLFSG FVNAALAYKA 


ARARAQQS 

« Hide

References

[1]"Complete sequence of Chromohalobacter salexigens DSM 3043."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Saunders E., Schmutz J. expand/collapse author list , Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Csonka L.N., O'Conner K., Vreeland R.H., Oren A., Vargas C., Nieto J., Arahal D.R., Goodner B., Wheeler C., Hall P., Ewing A., Benson L., McBeath D., Canovas D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000285 Genomic DNA. Translation: ABE57979.1.
RefSeqYP_572678.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID4029086.
GenomeReviewsGene locus Csal_0617 in contig CP000285_GR.
KEGGcsa:Csal_0617.
NMPDRfig|290398.4.peg.420.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1QZX9.
OMAQ1QZX9. EFNNAYR.

Enzyme and pathway databases

BioCycCSAL290398:CSAL_0617-MON.

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_CHRSD
AccessionPrimary (citable) accession number: Q1QZX9
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 27 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 · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents