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Protein

CTP synthase

Gene

pyrG

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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 sitei13Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei13UTP; alternateUniRule annotation1
Binding sitei54L-glutamineUniRule annotation1
Metal bindingi71MagnesiumUniRule annotation1
Binding sitei71ATPUniRule annotation1
Metal bindingi139MagnesiumUniRule annotation1
Binding sitei222Allosteric inhibitor CTP; alternateUniRule annotation1
Binding sitei222UTP; alternateUniRule annotation1
Binding sitei351L-glutamine; via carbonyl oxygenUniRule annotation1
Active sitei378Nucleophile; for glutamine hydrolysisUniRule annotation1
Binding sitei402L-glutamineUniRule annotation1
Binding sitei459L-glutamine; via amide nitrogenUniRule annotation1
Active sitei505UniRule annotation1
Active sitei507UniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi14 – 19ATPUniRule annotation6
Nucleotide bindingi146 – 148Allosteric inhibitor CTPUniRule annotation3
Nucleotide bindingi186 – 191Allosteric inhibitor CTP; alternateUniRule annotation6
Nucleotide bindingi186 – 191UTP; 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:PH1792
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001382671 – 537CTP synthaseAdd BLAST537

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi70601.PH1792.

Structurei

3D structure databases

ProteinModelPortaliO59456.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini290 – 532Glutamine amidotransferase type-1UniRule annotationAdd BLAST243

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 265Amidoligase domainUniRule annotationAdd BLAST265
Regioni379 – 382L-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

eggNOGiarCOG00063. Archaea.
COG0504. LUCA.
HOGENOMiHOG000077514.
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. 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.

O59456-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKFIFVTGG VVSGLGKGIT SASIGLLMKA RGYKTTNIKI DPYINYDAGT
60 70 80 90 100
MNPYQHGEVF VLDDGGEVDL DLGNYERFLD TNLTFEHNIT TGKVYSTVIE
110 120 130 140 150
KERRGEYLGA TVQVIPHITD EIKRRIREIA KDYDIVVVEI GGTVGDIESM
160 170 180 190 200
PFLEAARQMQ LEEGRENVAF VHVTYVPKLK VVGEQKTKPT QHSVKELRSL
210 220 230 240 250
GIQPDAIVAR SEDPLEEEAR KKISLFTNVP REAVVSAYDV EDTYEVPLLL
260 270 280 290 300
EREGLGKYLI KRLKLEDREP DLREWEKMVA KYKALKETVE IAIVGKYVKL
310 320 330 340 350
TDSYLSIKEA LKHASVSNDV KVKIRWIEAE DIEEHGTKLL EGVDGIIVPG
360 370 380 390 400
GFGARGAEGK IMTIKYAREN DIPFLGICFG FQLTVVEFAR NVLGMKGAHS
410 420 430 440 450
TEIDPQTPYP VVDLMPEQRN LEKLGGTMRL GAYPVKIKKG TLAYRLYKKE
460 470 480 490 500
LVYERHRHRW EVNPDYIEAF EKAGLVFSGV AGDDERRMEI LELPDKRYFI
510 520 530
ATQFHPEFKS RPMRPAPVFH GLVRAAKEYK QEKNATN
Length:537
Mass (Da):60,803
Last modified:October 19, 2002 - v2
Checksum:iD15DDB10CFF29004
GO

Sequence cautioni

The sequence BAA30911 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30911.1. Different initiation.
PIRiH71189.
RefSeqiWP_010885855.1. NC_000961.1.

Genome annotation databases

EnsemblBacteriaiBAA30911; BAA30911; BAA30911.
GeneIDi1442637.
KEGGipho:PH1792.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30911.1. Different initiation.
PIRiH71189.
RefSeqiWP_010885855.1. NC_000961.1.

3D structure databases

ProteinModelPortaliO59456.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1792.

Protein family/group databases

MEROPSiC26.964.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30911; BAA30911; BAA30911.
GeneIDi1442637.
KEGGipho:PH1792.

Phylogenomic databases

eggNOGiarCOG00063. Archaea.
COG0504. LUCA.
HOGENOMiHOG000077514.
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. 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_PYRHO
AccessioniPrimary (citable) accession number: O59456
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: November 30, 2016
This is version 102 of the entry and version 2 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

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.