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Protein

CTP synthase

Gene

pyrG

Organism
Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
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)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei13 – 131Allosteric inhibitor CTP; alternateUniRule annotation
Binding sitei13 – 131UTP; alternateUniRule annotation
Binding sitei54 – 541L-glutamineUniRule annotation
Metal bindingi71 – 711MagnesiumUniRule annotation
Binding sitei71 – 711ATPUniRule annotation
Metal bindingi139 – 1391MagnesiumUniRule annotation
Binding sitei222 – 2221Allosteric inhibitor CTP; alternateUniRule annotation
Binding sitei222 – 2221UTP; alternateUniRule annotation
Binding sitei353 – 3531L-glutamine; via carbonyl oxygenUniRule annotation
Active sitei380 – 3801Nucleophile; for glutamine hydrolysisUniRule annotation
Binding sitei404 – 4041L-glutamineUniRule annotation
Binding sitei469 – 4691L-glutamine; via amide nitrogenUniRule annotation
Active sitei514 – 5141UniRule annotation
Active sitei516 – 5161UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi14 – 196ATPUniRule annotation
Nucleotide bindingi146 – 1483Allosteric inhibitor CTPUniRule annotation
Nucleotide bindingi186 – 1916Allosteric inhibitor CTP; alternateUniRule annotation
Nucleotide bindingi186 – 1916UTP; alternateUniRule annotation

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:BMEI0849
OrganismiBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094)
Taxonomic identifieri224914 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella
Proteomesi
  • UP000000419 Componenti: Chromosome I

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 542542CTP synthasePRO_0000138167Add
BLAST

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi224914.BAWG_2820.

Structurei

3D structure databases

ProteinModelPortaliQ8YHF2.
SMRiQ8YHF2. Positions 2-540.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini291 – 541251Glutamine amidotransferase type-1UniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 265265Amidoligase domainUniRule annotationAdd
BLAST
Regioni381 – 3844L-glutamine bindingUniRule annotation

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.
OMAiMRLGEYE.
OrthoDBiEOG6RC3NR.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
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.

Q8YHF2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MARYVFITGG VVSSLGKGIA AAALAALLQA RGYRVRIRKL DPYLNVDPGT
60 70 80 90 100
MSPYQHGEVF VTDDGAETDL DLGHYERFTG RPANQQDNIT TGRIYRNIIE
110 120 130 140 150
KERRGDYLGA TVQVIPHVTD EIKNFVLEGN EDYDFVLCEI GGTVGDIEAM
160 170 180 190 200
PFLEAIRQLG NELPRGTAVY IHLTLMPYIP AAGELKTKPT QHSVKELRSI
210 220 230 240 250
GIAPDILLVR ADREIPESER RKLSLFCNVR ESAVIQALDV ATIYDVPIAY
260 270 280 290 300
HKEGLDSEVL SAFGIDPAPK PRMDRWEEVS HRLHNPEGEV TIAVVGKYTG
310 320 330 340 350
LKDAYKSLIE ALHHGGLANK VKVNLDWIEA EVFESEDPAP YLEKVHGILV
360 370 380 390 400
PGGFGERGAE GKILAAKFAR ERKVPYFGIC FGMQMACIEA ARNLVGIEDA
410 420 430 440 450
SSSEFDPTRE PVVGLMTEWL KGNMLEKRAA AGDLGGTMRL GAYEAVLKPD
460 470 480 490 500
SKIAQIYGST DIHERHRHRY EVNIDYKDRL EAAGLNFAGM SPDGVLPETV
510 520 530 540
EYADHPWFIG VQYHPELKSR PFEPHPLFAS FIEAAIEQSR LV
Length:542
Mass (Da):60,135
Last modified:March 1, 2002 - v1
Checksum:i30FE1EB1F908493E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52030.1.
PIRiAC3358.
RefSeqiWP_004683844.1. NZ_GG703780.1.

Genome annotation databases

EnsemblBacteriaiAAL52030; AAL52030; BMEI0849.
KEGGibme:BMEI0849.
PATRICi17801877. VBIBruMel146950_3258.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE008917 Genomic DNA. Translation: AAL52030.1.
PIRiAC3358.
RefSeqiWP_004683844.1. NZ_GG703780.1.

3D structure databases

ProteinModelPortaliQ8YHF2.
SMRiQ8YHF2. Positions 2-540.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi224914.BAWG_2820.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL52030; AAL52030; BMEI0849.
KEGGibme:BMEI0849.
PATRICi17801877. VBIBruMel146950_3258.

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
KOiK01937.
OMAiMRLGEYE.
OrthoDBiEOG6RC3NR.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
3.40.50.880. 1 hit.
HAMAPiMF_01227. PyrG.
InterProiIPR029062. Class_I_gatase-like.
IPR004468. CTP_synthase.
IPR017456. CTP_synthase_N.
IPR017926. GATASE.
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...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 16M / ATCC 23456 / NCTC 10094.

Entry informationi

Entry nameiPYRG_BRUME
AccessioniPrimary (citable) accession number: Q8YHF2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 90 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

Documents

  1. Brucella melitensis
    Brucella melitensis (strain 16M): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. 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.