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UniProtKB - P13242 (PYRG_BACSU)
Protein
CTP synthase
Gene
pyrG
Organism
Bacillus subtilis (strain 168)
Status
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 annotationMiscellaneous
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
- EC:6.3.4.2UniRule annotation
Activity 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
: CTP biosynthesis via de novo pathway Pathwayi
This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.UniRule annotation 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 key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Binding sitei | 13 | CTP; allosteric inhibitor; alternateUniRule annotation | 1 | |
Binding sitei | 13 | UTP; alternateUniRule annotation | 1 | |
Binding sitei | 54 | L-glutamineUniRule annotation | 1 | |
Metal bindingi | 71 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 71 | ATPUniRule annotation | 1 | |
Metal bindingi | 141 | MagnesiumUniRule annotation | 1 | |
Binding sitei | 224 | CTP; allosteric inhibitor; alternateUniRule annotation | 1 | |
Binding sitei | 224 | UTP; alternateUniRule annotation | 1 | |
Binding sitei | 354 | L-glutamine; via carbonyl oxygenUniRule annotation | 1 | |
Active sitei | 381 | Nucleophile; for glutamine hydrolysisUniRule annotation | 1 | |
Binding sitei | 405 | L-glutamineUniRule annotation | 1 | |
Binding sitei | 462 | L-glutamine; via amide nitrogenUniRule annotation | 1 | |
Active sitei | 507 | UniRule annotation | 1 | |
Active sitei | 509 | UniRule annotation | 1 |
Regions
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Nucleotide bindingi | 14 – 19 | ATPUniRule annotation | 6 | |
Nucleotide bindingi | 148 – 150 | CTP; allosteric inhibitorUniRule annotation | 3 | |
Nucleotide bindingi | 188 – 193 | CTP; allosteric inhibitor; alternateUniRule annotation | 6 | |
Nucleotide bindingi | 188 – 193 | UTP; alternateUniRule annotation | 6 |
GO - Molecular functioni
- ATP binding Source: UniProtKB-KW
- CTP synthase activity Source: GO_Central
- identical protein binding Source: GO_Central
- metal ion binding Source: UniProtKB-KW
GO - Biological processi
- 'de novo' CTP biosynthetic process Source: UniProtKB-UniPathway
- CTP biosynthetic process Source: GO_Central
- glutamine metabolic process Source: UniProtKB-KW
- pyrimidine nucleobase biosynthetic process Source: GO_Central
Keywordsi
Molecular function | Ligase |
Biological process | Pyrimidine biosynthesis |
Ligand | ATP-binding, Magnesium, Metal-binding, Nucleotide-binding |
Enzyme and pathway databases
BioCyci | BSUB:BSU37150-MONOMER |
UniPathwayi | UPA00159;UER00277 |
Protein family/group databases
MEROPSi | C26.964 |
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 Synonyms:ctrA Ordered Locus Names:BSU37150 |
Organismi | Bacillus subtilis (strain 168) |
Taxonomic identifieri | 224308 [NCBI] |
Taxonomic lineagei | Bacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000138165 | 1 – 535 | CTP synthaseAdd BLAST | 535 |
Proteomic databases
jPOSTi | P13242 |
PaxDbi | P13242 |
PRIDEi | P13242 |
Interactioni
Subunit structurei
Homotetramer.
UniRule annotationGO - Molecular functioni
- identical protein binding Source: GO_Central
Protein-protein interaction databases
STRINGi | 224308.BSU37150 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 292 – 534 | Glutamine amidotransferase type-1UniRule annotationAdd BLAST | 243 |
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 1 – 267 | Amidoligase domainUniRule annotationAdd BLAST | 267 | |
Regioni | 382 – 385 | L-glutamine bindingUniRule annotation | 4 |
Sequence similaritiesi
Belongs to the CTP synthase family.UniRule annotation
Keywords - Domaini
Glutamine amidotransferasePhylogenomic databases
eggNOGi | COG0504, Bacteria |
InParanoidi | P13242 |
OMAi | EFNNAYR |
PhylomeDBi | P13242 |
Family and domain databases
CDDi | cd03113, CTPS_N, 1 hit cd01746, GATase1_CTP_Synthase, 1 hit |
Gene3Di | 3.40.50.300, 1 hit 3.40.50.880, 1 hit |
HAMAPi | MF_01227, PyrG, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR11550, PTHR11550, 1 hit |
Pfami | View protein in Pfam PF06418, CTP_synth_N, 1 hit PF00117, GATase, 1 hit |
SUPFAMi | SSF52317, SSF52317, 1 hit SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR00337, PyrG, 1 hit |
PROSITEi | View protein in PROSITE PS51273, GATASE_TYPE_1, 1 hit |
i Sequence
Sequence statusi: Complete.
P13242-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MTKYIFVTGG VVSSLGKGIV AASLGRLLKN RGLNVTIQKF DPYINVDPGT
60 70 80 90 100
MSPYQHGEVF VTDDGAETDL DLGHYERFID INLNKFSNVT TGKIYSTVLK
110 120 130 140 150
KERRGDYLGG TVQVIPHITN ELKDRVYRAG KETNADVVIT EIGGTVGDIE
160 170 180 190 200
SLPFLEAIRQ MKSDIGRENV MYIHCTLVPY IKAAGELKTK PTQHSVKELR
210 220 230 240 250
SLGIQPNIIV VRTEMPISQD MKDKIALFCD IDTKAVIECE DADNLYSIPL
260 270 280 290 300
ELQKQGLDKL VCEHMKLACK EAEMSEWKEL VNKVSNLSQT ITIGLVGKYV
310 320 330 340 350
ELPDAYISVV ESLRHAGYAF DTDVKVKWIN AEEVTENNIA ELTSGTDGII
360 370 380 390 400
VPGGFGDRGV EGKIVATKYA RENNIPFLGI CLGMQVASIE YARNVLGLKG
410 420 430 440 450
AHSAEIDPST QYPIIDLLPE QKDVEDLGGT LRLGLYPCKL EEGTKAFEVY
460 470 480 490 500
QDEVVYERHR HRYEFNNEFR QQMEEQGFVF SGTSPDGRLV EIIELKDHPW
510 520 530
FVASQFHPEF KSRPTRPQPL FKGFIGASVE AANQK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22039 Unassigned DNA Translation: AAA16801.1 Z49782 Genomic DNA Translation: CAA89870.1 AL009126 Genomic DNA Translation: CAB15743.1 |
PIRi | A32354, SYBSTP |
RefSeqi | NP_391596.1, NC_000964.3 WP_003227612.1, NZ_JNCM01000034.1 |
Genome annotation databases
EnsemblBacteriai | CAB15743; CAB15743; BSU_37150 |
GeneIDi | 937044 |
KEGGi | bsu:BSU37150 |
PATRICi | fig|224308.179.peg.4024 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | M22039 Unassigned DNA Translation: AAA16801.1 Z49782 Genomic DNA Translation: CAA89870.1 AL009126 Genomic DNA Translation: CAB15743.1 |
PIRi | A32354, SYBSTP |
RefSeqi | NP_391596.1, NC_000964.3 WP_003227612.1, NZ_JNCM01000034.1 |
3D structure databases
SMRi | P13242 |
ModBasei | Search... |
Protein-protein interaction databases
STRINGi | 224308.BSU37150 |
Protein family/group databases
MEROPSi | C26.964 |
Proteomic databases
jPOSTi | P13242 |
PaxDbi | P13242 |
PRIDEi | P13242 |
Genome annotation databases
EnsemblBacteriai | CAB15743; CAB15743; BSU_37150 |
GeneIDi | 937044 |
KEGGi | bsu:BSU37150 |
PATRICi | fig|224308.179.peg.4024 |
Phylogenomic databases
eggNOGi | COG0504, Bacteria |
InParanoidi | P13242 |
OMAi | EFNNAYR |
PhylomeDBi | P13242 |
Enzyme and pathway databases
UniPathwayi | UPA00159;UER00277 |
BioCyci | BSUB:BSU37150-MONOMER |
Family and domain databases
CDDi | cd03113, CTPS_N, 1 hit cd01746, GATase1_CTP_Synthase, 1 hit |
Gene3Di | 3.40.50.300, 1 hit 3.40.50.880, 1 hit |
HAMAPi | MF_01227, PyrG, 1 hit |
InterProi | View 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 |
PANTHERi | PTHR11550, PTHR11550, 1 hit |
Pfami | View protein in Pfam PF06418, CTP_synth_N, 1 hit PF00117, GATase, 1 hit |
SUPFAMi | SSF52317, SSF52317, 1 hit SSF52540, SSF52540, 1 hit |
TIGRFAMsi | TIGR00337, PyrG, 1 hit |
PROSITEi | View protein in PROSITE PS51273, GATASE_TYPE_1, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | PYRG_BACSU | |
Accessioni | P13242Primary (citable) accession number: P13242 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | January 1, 1990 |
Last sequence update: | January 1, 1990 | |
Last modified: | February 23, 2022 | |
This is version 152 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Reference proteomeDocuments
- PATHWAY comments
Index of metabolic and biosynthesis pathways - SIMILARITY comments
Index of protein domains and families