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Protein

CTP synthase

Gene

pyrG

Organism
Frankia sp. (strain CcI3)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen. Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates.UniRule annotation

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.UniRule annotation

Enzyme regulationi

Allosterically activated by GTP, when glutamine is the substrate; GTP has no effect on the reaction when ammonia is the substrate. The allosteric effector GTP functions by stabilizing the protein conformation that binds the tetrahedral intermediate(s) formed during glutamine hydrolysis. Inhibited by the product CTP, via allosteric rather than competitive inhibition.UniRule annotation

Pathwayi: CTP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. no protein annotated in this organism
  2. CTP synthase (pyrG)
This subpathway is part of the pathway CTP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes CTP from UDP, the pathway CTP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei18Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei18UTP; alternateUniRule annotation1
Metal bindingi76MagnesiumUniRule annotation1
Binding sitei76ATPUniRule annotation1
Metal bindingi145MagnesiumUniRule annotation1
Binding sitei228Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei228UTP; alternateUniRule annotation1
Binding sitei359L-glutamine; via carbonyl oxygenUniRule annotation1
Active sitei386Nucleophile; for glutamine hydrolysisUniRule annotation1
Binding sitei410L-glutamineUniRule annotation1
Binding sitei471L-glutamine; via amide nitrogenUniRule annotation1
Active sitei518UniRule annotation1
Active sitei520UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi19 – 24ATPUniRule annotation6
Nucleotide bindingi152 – 154Allosteric inhibitor CTPUniRule annotation3
Nucleotide bindingi192 – 197Allosteric inhibitor CTP; alternateUniRule annotation6
Nucleotide bindingi192 – 197UTP; alternateUniRule annotation6

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.

Protein family/group databases

MEROPSiC26.964.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP synthaseUniRule annotation (EC:6.3.4.2UniRule annotation)
Alternative name(s):
Cytidine 5'-triphosphate synthaseUniRule annotation
Cytidine triphosphate synthetaseUniRule annotation
Short name:
CTP synthetaseUniRule annotation
Short name:
CTPSUniRule annotation
UTP--ammonia ligaseUniRule annotation
Gene namesi
Name:pyrGUniRule annotation
Ordered Locus Names:Francci3_3157
OrganismiFrankia sp. (strain CcI3)
Taxonomic identifieri106370 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaFrankialesFrankiaceaeFrankia
Proteomesi
  • UP000001937 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002661231 – 608CTP synthaseAdd BLAST608

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi106370.Francci3_3157.

Structurei

3D structure databases

ProteinModelPortaliQ2J878.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini296 – 545Glutamine amidotransferase type-1UniRule annotationAdd BLAST250

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 271Amidoligase domainUniRule annotationAdd BLAST271
Regioni387 – 390L-glutamine bindingUniRule annotation4

Sequence similaritiesi

Belongs to the CTP synthase family.UniRule annotation
Contains 1 glutamine amidotransferase type-1 domain.UniRule annotation

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
KOiK01937.
OMAiTMRLGEY.
OrthoDBiPOG091H02IX.

Family and domain databases

CDDicd01746. GATase1_CTP_Synthase. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR033828. GATase1_CTP_Synthase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q2J878-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQAHITKHI FVTGGVASSL GKGLTASSLG RLLKARGLRV TMQKLDPYLN
60 70 80 90 100
VDPGTMNPFQ HGEVFVTDDG AETDLDIGHY ERFLDVSLDG SANVTTGQVY
110 120 130 140 150
SAVIARERRG GYLGQTVQVV PHITDEIKDR IRRLADDSVD VVITEVGGTV
160 170 180 190 200
GDIESLPYLE AIRQVRHEVG RDNALTVHVS LVPYLAPSGE LKTKPTQHSV
210 220 230 240 250
AALRSIGLQP DAVVCRSDRP LPDSLKKKIA MMCDVDDEAV VGAPDASSIY
260 270 280 290 300
DIPRVLHREG LDAYVVRRLG LSFRDVDWTE WDTLLRRVHH PANTATIAIV
310 320 330 340 350
GKYVDLPDAY LSVTEALRAG AFATDTRVDL RWVTSDECSS PDATATLLDG
360 370 380 390 400
IDGVIVPGGF GVRGIEGKLT ALRHARENGI PTLGICLGLQ CMVIEAARSL
410 420 430 440 450
AGLEAANSTE FVPETPHPVI STMADQHEVV AGTRDMGGTM RLGLYSCVLA
460 470 480 490 500
PGTLAQREYG AAEVAERHRH RYEVNNDYRH RLAAAGLVFS GTSPDGRLVE
510 520 530 540 550
VVELPADVHP YYVGTQAHPE FRSRPTRAHP LFRGLVAAAV AHADRRRGML
560 570 580 590 600
PVDLPSEDAP TPENGVPENG AAQTRGVTAG RSGGSIRRGA SASRPSVSSN

GTAALVSP
Length:608
Mass (Da):65,190
Last modified:March 7, 2006 - v1
Checksum:i9450982D0FA4BAD0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000249 Genomic DNA. Translation: ABD12514.1.
RefSeqiWP_011437542.1. NC_007777.1.

Genome annotation databases

EnsemblBacteriaiABD12514; ABD12514; Francci3_3157.
KEGGifra:Francci3_3157.
PATRICi21929624. VBIFraSp10456_3427.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000249 Genomic DNA. Translation: ABD12514.1.
RefSeqiWP_011437542.1. NC_007777.1.

3D structure databases

ProteinModelPortaliQ2J878.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi106370.Francci3_3157.

Protein family/group databases

MEROPSiC26.964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABD12514; ABD12514; Francci3_3157.
KEGGifra:Francci3_3157.
PATRICi21929624. VBIFraSp10456_3427.

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
KOiK01937.
OMAiTMRLGEY.
OrthoDBiPOG091H02IX.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.

Family and domain databases

CDDicd01746. GATase1_CTP_Synthase. 1 hit.
Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG. 1 hit.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
IPR033828. GATase1_CTP_Synthase.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11550. PTHR11550. 1 hit.
PfamiPF06418. CTP_synth_N. 1 hit.
PF00117. GATase. 1 hit.
[Graphical view]
SUPFAMiSSF52317. SSF52317. 1 hit.
SSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR00337. PyrG. 1 hit.
PROSITEiPS51273. GATASE_TYPE_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPYRG_FRASC
AccessioniPrimary (citable) accession number: Q2J878
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: March 7, 2006
Last modified: November 30, 2016
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

CTPSs have evolved a hybrid strategy for distinguishing between UTP and CTP. The overlapping regions of the product feedback inhibitory and substrate sites recognize a common feature in both compounds, the triphosphate moiety. To differentiate isosteric substrate and product pyrimidine rings, an additional pocket far from the expected kinase/ligase catalytic site, specifically recognizes the cytosine and ribose portions of the product inhibitor.UniRule annotation

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.