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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: -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

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

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

Keywordsi

Molecular functionLigase
Biological processPyrimidine biosynthesis
LigandATP-binding, Magnesium, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciPHOR70601:G1G39-1737-MONOMER
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
SMRiO59456
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

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiarCOG00063 Archaea
COG0504 LUCA
HOGENOMiHOG000077514
KOiK01937
OMAiEFNNAYR
OrthoDBiPOG093Z01Z8

Family and domain databases

CDDicd01746 GATase1_CTP_Synthase, 1 hit
Gene3Di3.40.50.880, 1 hit
HAMAPiMF_01227 PyrG, 1 hit
InterProiView protein in InterPro
IPR029062 Class_I_gatase-like
IPR004468 CTP_synthase
IPR017456 CTP_synthase_N
IPR017926 GATASE
IPR033828 GATase1_CTP_Synthase
IPR027417 P-loop_NTPase
PANTHERiPTHR11550 PTHR11550, 1 hit
PfamiView protein in Pfam
PF06418 CTP_synth_N, 1 hit
PF00117 GATase, 1 hit
SUPFAMiSSF52317 SSF52317, 1 hit
SSF52540 SSF52540, 1 hit
TIGRFAMsiTIGR00337 PyrG, 1 hit
PROSITEiView protein in PROSITE
PS51273 GATASE_TYPE_1, 1 hit

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

Entry informationi

Entry nameiPYRG_PYRHO
AccessioniPrimary (citable) accession number: O59456
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 19, 2002
Last modified: April 25, 2018
This is version 108 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
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Main funding by: National Institutes of Health