Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

CTP synthase

Gene

pyrG

Organism
Coxiella burnetii (strain RSA 493 / Nine Mile phase I)
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
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 sitei469L-glutamine; via amide nitrogenUniRule annotation1
Active sitei514UniRule annotation1
Active sitei516UniRule 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

BioCyciCBUR227377:G1G0B-1651-MONOMER
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:CBU_1682
OrganismiCoxiella burnetii (strain RSA 493 / Nine Mile phase I)
Taxonomic identifieri227377 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaLegionellalesCoxiellaceaeCoxiella
Proteomesi
  • UP000002671 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002661011 – 555CTP synthaseAdd BLAST555

Proteomic databases

PRIDEiQ83B36

Interactioni

Subunit structurei

Homotetramer.UniRule annotation

Protein-protein interaction databases

STRINGi227377.CBU_1682

Structurei

3D structure databases

ProteinModelPortaliQ83B36
SMRiQ83B36
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini290 – 541Glutamine amidotransferase type-1UniRule annotationAdd BLAST252

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

eggNOGiENOG4105C8D Bacteria
COG0504 LUCA
HOGENOMiHOG000077515
KOiK01937
OMAiEFNNAYR

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.

Q83B36-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTRYIFITGG VVSSLGKGIT SASLGAILEA QGLTVTLLKL DPYINVDPGT
60 70 80 90 100
MSPFQHGEVF VTEDGAETDL DLGHYERFVN ATMTRKNNFT TGRVYADVIR
110 120 130 140 150
KERRGDYLGG TIQVIPHITD EIKAKIREGA DGADVALVEV GGTVGDIESL
160 170 180 190 200
PFLEAIRQMR IELGDQQTLF IHLTLVPYVA VAGEIKTKPT QHSVKELRSI
210 220 230 240 250
GIQPDILVCR SEQPLPDAER AKIALFTNVP EPSVISLSDV KSIYEIPLIL
260 270 280 290 300
RDQGLGNRVC EKLNIKATAA DLDDWKKVVQ AQKNPRHTVT VAVVGKYVDL
310 320 330 340 350
EDSYKSLSEA LIHAGIHTQT RVVIEYIDSE AIELHGTELL KKVDAILVPG
360 370 380 390 400
GFGSRGIEGK ILAAQYAREN GIPYFGICLG MQIAIIEFAR DKAQMENANS
410 420 430 440 450
TEFDPKTPFP VVALVSEWMA KEGIIEKRKW GDDLGGTMRL GGQPCRLKID
460 470 480 490 500
SLARRLYGED RVIERHRHRY EVNNDLIGEL EKKGLVISGR SIDDRLVEMI
510 520 530 540 550
ELADHPWFVG CQFHPEFTST PRKGHPLFIG FIKAGLAAKE AKKAVLAAPS

QEKTD
Length:555
Mass (Da):61,224
Last modified:June 1, 2003 - v1
Checksum:i2BA610F28796742C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE016828 Genomic DNA Translation: AAO91178.1
RefSeqiNP_820664.1, NC_002971.3
WP_010958369.1, NC_002971.4

Genome annotation databases

EnsemblBacteriaiAAO91178; AAO91178; CBU_1682
GeneIDi1209593
KEGGicbu:CBU_1682
PATRICifig|227377.7.peg.1671

Similar proteinsi

Entry informationi

Entry nameiPYRG_COXBU
AccessioniPrimary (citable) accession number: Q83B36
Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 12, 2006
Last sequence update: June 1, 2003
Last modified: February 28, 2018
This is version 95 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Coxiella burnetii
    Coxiella burnetii (strain RSA 493): entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health