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Protein

CTP synthase

Gene

pyrG

Organism
Treponema pallidum (strain Nichols)
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), 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 sitei14Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei14UTP; alternateUniRule annotation1
Binding sitei55L-glutamineUniRule annotation1
Metal bindingi72MagnesiumUniRule annotation1
Binding sitei72ATPUniRule annotation1
Metal bindingi142MagnesiumUniRule annotation1
Binding sitei225Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei225UTP; alternateUniRule annotation1
Binding sitei396L-glutamine; via carbonyl oxygenUniRule annotation1
Active sitei423Nucleophile; for glutamine hydrolysisUniRule annotation1
Binding sitei447L-glutamineUniRule annotation1
Binding sitei503L-glutamine; via amide nitrogenUniRule annotation1
Active sitei548UniRule annotation1
Active sitei550UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi15 – 20ATPUniRule annotation6
Nucleotide bindingi149 – 151Allosteric inhibitor CTPUniRule annotation3
Nucleotide bindingi189 – 194Allosteric inhibitor CTP; alternateUniRule annotation6
Nucleotide bindingi189 – 194UTP; 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.

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:TP_0305
OrganismiTreponema pallidum (strain Nichols)
Taxonomic identifieri243276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesSpirochaetalesSpirochaetaceaeTreponema
Proteomesi
  • UP000000811 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001382441 – 577CTP synthaseAdd BLAST577

Proteomic databases

PRIDEiO83327.

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

IntActiO83327. 4 interactors.
MINTiMINT-6479806.
STRINGi243276.TP0305.

Structurei

3D structure databases

ProteinModelPortaliO83327.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini333 – 575Glutamine amidotransferase type-1UniRule annotationAdd BLAST243

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 268Amidoligase domainUniRule annotationAdd BLAST268
Regioni424 – 427L-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.
KOiK01937.
OMAiTMRLGEY.

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. 2 hits.
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.

O83327-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDPAFIFITG GVVSSLGKGI AAGAIGLLLK SRGISVVNQK FDPYLNGDPG
60 70 80 90 100
TMNPYQHGEV FVTQDGGETD LDLGHYERFT DVPSSRFNST TAGSVYRAIL
110 120 130 140 150
DRERAGGYGG ATVQVIPHVT DEIQARIRAA AATTGARVVI TEIGGTVGDI
160 170 180 190 200
ESLPFIEAIR QIRRVLGKER CLFIHLGLVP YLPSCGEMKT KPLQHSVKEL
210 220 230 240 250
LGLGVQPDVI LCRSERHITD AVREKLSLFC NVERRAIVEN VTARSIYEVP
260 270 280 290 300
LLLEAEGLGA LLCERLRLFD TCCGGQVARN LGAGGAQSAV LGAGGTVRTD
310 320 330 340 350
GGLHPAAGQG AEPDLTAWRA MVRALYYPRR ELTVALVGKY VSLADAYLSV
360 370 380 390 400
SEALTAAGIC HRARVDMRWI DAEEICSVQD AGHALADADA LVIPGGFGVR
410 420 430 440 450
GIEGMICAVS HARVQNLPYL GICLGMQIAV IEFARNVLLL ASAHSREFAV
460 470 480 490 500
DTPHPVVDLL PGCVDTPTGG SLRLGQYRCL LAEGSRARAL YGRGEVWERH
510 520 530 540 550
RHRYGLNAAY RARFEASALR PVGVDSDCGA VEVVEHGEHP WFFGVQFHPE
560 570
FCSRPNRAHP LFRALVAAGL ERKDSRS
Length:577
Mass (Da):62,147
Last modified:November 1, 1998 - v1
Checksum:iAFAD747EA85932D2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA. Translation: AAC65292.1.
PIRiC71342.
RefSeqiWP_010881754.1. NC_021490.2.

Genome annotation databases

EnsemblBacteriaiAAC65292; AAC65292; TP_0305.
GeneIDi2610727.
KEGGitpa:TP_0305.
PATRICi20530601. VBITrePal57110_0323.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000520 Genomic DNA. Translation: AAC65292.1.
PIRiC71342.
RefSeqiWP_010881754.1. NC_021490.2.

3D structure databases

ProteinModelPortaliO83327.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiO83327. 4 interactors.
MINTiMINT-6479806.
STRINGi243276.TP0305.

Proteomic databases

PRIDEiO83327.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC65292; AAC65292; TP_0305.
GeneIDi2610727.
KEGGitpa:TP_0305.
PATRICi20530601. VBITrePal57110_0323.

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
KOiK01937.
OMAiTMRLGEY.

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. 2 hits.
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_TREPA
AccessioniPrimary (citable) accession number: O83327
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: November 1, 1998
Last modified: November 30, 2016
This is version 100 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.