Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q2A2S0 (PYRG_FRATH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:
CTP synthase

EC=6.3.4.2
Alternative name(s):
CTP synthetase
UTP--ammonia ligase
Gene names
Name:pyrG
Ordered Locus Names:FTL_1311
OrganismFrancisella tularensis subsp. holarctica (strain LVS) [Complete proteome] [HAMAP]
Taxonomic identifier376619 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaThiotrichalesFrancisellaceaeFrancisella

Protein attributes

Sequence length546 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-Rule MF_01227

Catalytic activity

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

Enzyme regulation

Allosterically activated by GTP, when glutamine is the substrate. Inhibited by CTP By similarity. HAMAP-Rule MF_01227

Pathway

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

Subunit structure

Homotetramer By similarity. HAMAP-Rule MF_01227

Sequence similarities

Belongs to the CTP synthase family.

Contains 1 glutamine amidotransferase type-1 domain.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   DomainGlutamine amidotransferase
   LigandATP-binding
Nucleotide-binding
   Molecular functionLigase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' CTP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

glutamine metabolic process

Inferred from electronic annotation. Source: HAMAP

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

CTP synthase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 546546CTP synthase HAMAP-Rule MF_01227
PRO_0000266119

Regions

Domain294 – 546253Glutamine amidotransferase type-1
Region1 – 256256Aminator domain HAMAP-Rule MF_01227

Sites

Active site3831Nucleophile By similarity
Active site5191 By similarity
Active site5211 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2A2S0 [UniParc].

Last modified April 4, 2006. Version 1.
Checksum: 60D0C7DF40286E9D

FASTA54661,042
        10         20         30         40         50         60 
MNSNTKIIFV TGGVVSSLGK GVTAASLATL LESRGLNVTM MKLDPYINVD PGTMSPLQHG 

        70         80         90        100        110        120 
EVFVTEDGAE TDLDLGHYER FIRNKMTQAN NFTTGKVYQS VLRRERKGDY LGATIQVIPH 

       130        140        150        160        170        180 
ITDEIKRRIC SGIADDVDVA IVEIGGTVGD IESQPFLEAI RQLRIELGRN RTLFVHLTLL 

       190        200        210        220        230        240 
PYIKVAGEIK TKPTQHSVKE LRGIGIQADV LVCRCEKKFD DSEKRKIALF TNVDQDCIFT 

       250        260        270        280        290        300 
AEDVDTIYEV PLKYNQQGFD AKLVELLNLN AKEADLSEWQ NVVNTIRDVK GEVIIAMVGK 

       310        320        330        340        350        360 
YVSLTEAYKS LNEALYNAGY KKGVKVKIKF VDSEDVNENN VESYFKDVAA ILVPGGFGSR 

       370        380        390        400        410        420 
GVEGKIISIK YARENQIPFL GICLGMQLAV IEYARNILGI KDAHSSELEP TTANPVIGLI 

       430        440        450        460        470        480 
TEWQAEDGTV HQRTHSSDLG GTMRLGGYKC VLKQGSRARE IYQADEVVER HRHRYEVNSN 

       490        500        510        520        530        540 
YVERLEEAGL IFSGRSEDNK LMELIEIPQH KWFIACQAHP EFTSTPRYGH KLFESYIQAA 


IENSNN 

« Hide

References

[1]"Complete genome sequence of Francisella tularensis LVS (Live Vaccine Strain)."
Chain P., Larimer F., Land M., Stilwagen S., Larsson P., Bearden S., Chu M., Oyston P., Forsman M., Andersson S., Lindler L., Titball R., Garcia E.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LVS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AM233362 Genomic DNA. Translation: CAJ79750.1.
RefSeqYP_513982.1. NC_007880.1.

3D structure databases

ProteinModelPortalQ2A2S0.
SMRQ2A2S0. Positions 4-545.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAJ79750; CAJ79750; FTL_1311.
GeneID3952302.
KEGGftl:FTL_1311.
PATRIC17943756. VBIFraTul90181_1427.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0504.
HOGENOMHOG000077515.
KOK01937.
OMATNEIKDR.
ProtClustDBPRK05380.

Enzyme and pathway databases

BioCycFTUL376619:GI22-1344-MONOMER.
UniPathwayUPA00159; UER00277.

Family and domain databases

HAMAPMF_01227. PyrG.
InterProIPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR11550. PTHR11550. 1 hit.
PfamPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
TIGRFAMsTIGR00337. PyrG. 1 hit.
PROSITEPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRG_FRATH
AccessionPrimary (citable) accession number: Q2A2S0
Entry history
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: April 4, 2006
Last modified: May 29, 2013
This is version 54 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