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Protein

CTP synthase

Gene

pyrG

Organism
Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the ATP-dependent amination of UTP to CTP with either L-glutamine or ammonia as the source of nitrogen (PubMed:21301086). Regulates intracellular CTP levels through interactions with the four ribonucleotide triphosphates (By similarity).UniRule annotation1 Publication

Catalytic activityi

ATP + UTP + L-glutamine = ADP + phosphate + CTP + L-glutamate.UniRule annotation1 Publication

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 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 sitei243ATP; via amide nitrogenUniRule annotation1
Binding sitei359L-glutamine; via carbonyl oxygenUniRule annotation1
Active sitei386Nucleophile; for glutamine hydrolysisUniRule annotation1
Binding sitei410L-glutamineUniRule annotation1
Binding sitei467L-glutamine; via amide nitrogenUniRule annotation1
Active sitei511UniRule annotation1
Active sitei513UniRule 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

BRENDAi6.3.4.2. 6163.
UniPathwayiUPA00159; UER00277.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP synthase1 PublicationUniRule annotation (EC:6.3.4.2UniRule annotation1 Publication)
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:SSO0201
OrganismiSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Taxonomic identifieri273057 [NCBI]
Taxonomic lineageiArchaeaCrenarchaeotaThermoproteiSulfolobalesSulfolobaceaeSulfolobus
Proteomesi
  • UP000001974 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001382701 – 535CTP synthaseAdd BLAST535

Interactioni

Subunit structurei

Homotetramer in the presence of ATP and UTP. The enzyme dissociates into homodimers in the absence of substrate nucleotides.1 Publication

Protein-protein interaction databases

STRINGi273057.SSO0201.

Structurei

Secondary structure

1535
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 9Combined sources6
Turni14 – 17Combined sources4
Helixi18 – 31Combined sources14
Beta strandi36 – 42Combined sources7
Beta strandi44 – 49Combined sources6
Helixi54 – 57Combined sources4
Helixi72 – 80Combined sources9
Helixi86 – 88Combined sources3
Beta strandi89 – 91Combined sources3
Helixi92 – 104Combined sources13
Turni105 – 110Combined sources6
Helixi115 – 134Combined sources20
Beta strandi137 – 143Combined sources7
Helixi150 – 152Combined sources3
Helixi153 – 166Combined sources14
Turni168 – 170Combined sources3
Beta strandi171 – 178Combined sources8
Turni183 – 185Combined sources3
Beta strandi186 – 188Combined sources3
Helixi191 – 203Combined sources13
Beta strandi208 – 216Combined sources9
Helixi220 – 229Combined sources10
Helixi234 – 236Combined sources3
Beta strandi237 – 241Combined sources5
Helixi246 – 248Combined sources3
Helixi249 – 256Combined sources8
Helixi258 – 265Combined sources8
Helixi276 – 286Combined sources11
Turni287 – 289Combined sources3
Beta strandi293 – 301Combined sources9
Helixi306 – 309Combined sources4
Helixi310 – 322Combined sources13
Beta strandi326 – 333Combined sources8
Helixi334 – 337Combined sources4
Beta strandi340 – 342Combined sources3
Turni345 – 349Combined sources5
Beta strandi352 – 356Combined sources5
Helixi365 – 378Combined sources14
Beta strandi382 – 385Combined sources4
Helixi387 – 398Combined sources12
Turni399 – 401Combined sources3
Turni409 – 411Combined sources3
Beta strandi418 – 421Combined sources4
Beta strandi425 – 427Combined sources3
Beta strandi437 – 445Combined sources9
Helixi450 – 455Combined sources6
Beta strandi457 – 466Combined sources10
Helixi472 – 480Combined sources9
Beta strandi484 – 488Combined sources5
Beta strandi494 – 498Combined sources5
Beta strandi505 – 510Combined sources6
Helixi512 – 515Combined sources4
Beta strandi518 – 520Combined sources3
Helixi523 – 532Combined sources10

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NVAX-ray2.50A/B1-535[»]
ProteinModelPortaliQ980S6.
SMRiQ980S6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ980S6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini302 – 535Glutamine amidotransferase type-1UniRule annotationAdd BLAST234

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 268Amidoligase domainUniRule annotationAdd BLAST268
Regioni387 – 390L-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.
InParanoidiQ980S6.
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.

Q980S6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNKYIVVTG GVLSSVGKGT LVASIGMLLK RRGYNVTAVK IDPYINVDAG
60 70 80 90 100
TMNPYMHGEV FVTEDGAETD LDLGHYERFM DVNMTKYNNI TAGKVYFEVI
110 120 130 140 150
KKEREGKYLG QTVQIIPHVT DQIKDMIRYA SKINNAEITL VEIGGTVGDI
160 170 180 190 200
ESLPFLEAVR QLKLEEGEDN VIFVHIALVE YLSVTGELKT KPLQHSVQEL
210 220 230 240 250
RRIGIQPDFI VGRATLPLDD ETRRKIALFT NVKVDHIVSS YDVETSYEVP
260 270 280 290 300
IILESQKLVS KILSRLKLED RQVDLTDWIS FVNNIKGINS KKTINIALVG
310 320 330 340 350
KYTKLKDSYI SIKEAIYHAS AYIGVRPKLI WIESTDLESD TKNLNEILGN
360 370 380 390 400
VNGIIVLPGF GSRGAEGKIK AIKYAREHNI PFLGICFGFQ LSIVEFARDV
410 420 430 440 450
LGLSEANSTE INPNTKDPVI TLLDEQKNVT QLGGTMRLGA QKIILKEGTI
460 470 480 490 500
AYQLYGKKVV YERHRHRYEV NPKYVDILED AGLVVSGISE NGLVEIIELP
510 520 530
SNKFFVATQA HPEFKSRPTN PSPIYLGFIR AVASL
Length:535
Mass (Da):59,760
Last modified:October 1, 2001 - v1
Checksum:iC4E4BDE58B3DADED
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40547.1.
PIRiD90161.
RefSeqiWP_009990444.1. NC_002754.1.

Genome annotation databases

EnsemblBacteriaiAAK40547; AAK40547; SSO0201.
GeneIDi27426496.
KEGGisso:SSO0201.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE006641 Genomic DNA. Translation: AAK40547.1.
PIRiD90161.
RefSeqiWP_009990444.1. NC_002754.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
3NVAX-ray2.50A/B1-535[»]
ProteinModelPortaliQ980S6.
SMRiQ980S6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi273057.SSO0201.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK40547; AAK40547; SSO0201.
GeneIDi27426496.
KEGGisso:SSO0201.

Phylogenomic databases

eggNOGiarCOG00063. Archaea.
COG0504. LUCA.
HOGENOMiHOG000077514.
InParanoidiQ980S6.
KOiK01937.
OMAiTMRLGEY.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.
BRENDAi6.3.4.2. 6163.

Miscellaneous databases

EvolutionaryTraceiQ980S6.

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_SULSO
AccessioniPrimary (citable) accession number: Q980S6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 19, 2002
Last sequence update: October 1, 2001
Last modified: November 30, 2016
This is version 94 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  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.