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Q2SXC7 (PYRG_BURTA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 44. 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:
CTP synthase

EC=6.3.4.2
Alternative name(s):
CTP synthetase
UTP--ammonia ligase
Gene names
Name:pyrG
Ordered Locus Names:BTH_I1892
OrganismBurkholderia thailandensis (strain E264 / ATCC 700388 / DSM 13276 / CIP 106301) [Complete proteome] [HAMAP]
Taxonomic identifier271848 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaBurkholderialesBurkholderiaceaeBurkholderiapseudomallei group

Protein attributes

Sequence length553 AA.
Sequence statusComplete.
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. HAMAP MF_01227

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. HAMAP MF_01227

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP MF_01227

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 – 553553CTP synthase HAMAP MF_01227
PRO_0000266086

Regions

Domain295 – 547253Glutamine amidotransferase type-1
Region1 – 257257Aminator domain HAMAP MF_01227

Sites

Active site3831Nucleophile By similarity
Active site5201 By similarity
Active site5221 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2SXC7 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 5D1CB23AAC3FF8F6

FASTA55361,095
        10         20         30         40         50         60 
MTKYVFVTGG VVSSLGKGIA AASLAAILES RGLKVTLLKL DPYINVDPGT MSPFQHGEVF 

        70         80         90        100        110        120 
VTEDGAETDL DLGHYERFIS TKMRKANNFT TGQIYESVIR KERRGDYLGK TVQVIPHITN 

       130        140        150        160        170        180 
EIQAFIERGA ASATCGEPDV AIVEIGGTVG DIESLPFLEA ARQMSLRLGR NSACFVHLTL 

       190        200        210        220        230        240 
VPFIATAGEL KTKPTQHSVQ KLREIGISPH VLLCRADRPI PDDESKKISL FSNVPEDAVI 

       250        260        270        280        290        300 
SVWDVDSIYK IPQMLHDQGL DRLICEELRL DPQPADLRMW SELVEKLQNP KHEVTIGMVG 

       310        320        330        340        350        360 
KYVDLTESYK SLIEALRHAS IHTSTKVNIE YIDSEELEAN GTASLAHLDA VLVPGGFGRR 

       370        380        390        400        410        420 
GTEGKIAAVR YAREAKVPYL GICLGMQLAV IEFARDVVGL KQANSTEFDP NTPERVVALI 

       430        440        450        460        470        480 
TEWYDREGKV EKRTEDSDLG GTMRLGSQRC PIKPGTLAEA IYGKDVNERH RHRYEVNNRF 

       490        500        510        520        530        540 
VPQLEAGGLV ISARTPSEDL PEMMELPRAM HPWFVGVQFH PEFTSTPRDG HPLFKSFVQA 

       550 
AIACQQARAG AKA 

« Hide

References

[1]"Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies."
Kim H.S., Schell M.A., Yu Y., Ulrich R.L., Sarria S.H., Nierman W.C., DeShazer D.
BMC Genomics 6:174-174(2005) [PubMed: 16336651] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: E264 / ATCC 700388 / DSM 13276 / CIP 106301.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000086 Genomic DNA. Translation: ABC37894.1.
RefSeqYP_442422.1. NC_007651.1.

3D structure databases

HSSPHSSP built from PDB template 2C5M based on UniProtKB P17812.
ProteinModelPortalQ2SXC7.
SMRQ2SXC7. Positions 2-549.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ2SXC7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3848784.
GenomeReviewsGene locus BTH_I1892 in contig CP000086_GR.
KEGGbte:BTH_I1892.
PATRIC19306810. VBIBurTha36512_4700.
TIGRBTH_I1892.

Phylogenomic databases

eggNOGCOG0504.
HOGENOMHBG597806.
OMARVTMQKL.
ProtClustDBPRK05380.

Enzyme and pathway databases

BioCycBTHA271848:BTH_I1892-MONOMER.

Family and domain databases

HAMAPMF_01227. PyrG.
[Tree]
InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE_1.
[Graphical view]
KOK01937.
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_BURTA
AccessionPrimary (citable) accession number: Q2SXC7
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: January 24, 2006
Last modified: January 25, 2012
This is version 44 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