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Protein

CTP synthase

Gene

pyrG

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 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.

Catalytic activityi

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

Enzyme regulationi

Allosterically activated by GTP, when glutamine is the substrate. Also activated by magnesium. Inhibited by CTP and by divalent metal ions such as copper and zinc.1 Publication

pH dependencei

Optimum pH is 8.7.

Pathwayi: CTP biosynthesis via de novo pathway

This protein is involved in step 2 of the subpathway that synthesizes CTP from UDP.
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
Active sitei379 – 3791NucleophileCurated
Active sitei515 – 5151By similarity
Active sitei517 – 5171By similarity

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • CTP synthase activity Source: EcoCyc
  • identical protein binding Source: EcoCyc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciEcoCyc:CTPSYN-MONOMER.
ECOL316407:JW2751-MONOMER.
MetaCyc:CTPSYN-MONOMER.
BRENDAi6.3.4.2. 2026.
UniPathwayiUPA00159; UER00277.

Protein family/group databases

MEROPSiC26.964.

Names & Taxonomyi

Protein namesi
Recommended name:
CTP synthase (EC:6.3.4.2)
Alternative name(s):
CTP synthetase
UTP--ammonia ligase
Gene namesi
Name:pyrG
Ordered Locus Names:b2780, JW2751
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10810. pyrG.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi349 – 3491V → S: 30% increase in both glutamine-dependent and ammonia-dependent activities. 1 Publication
Mutagenesisi352 – 3521G → P: Loss of glutamine-dependent activity, but no change in ammonia-dependent activity. 1 Publication
Mutagenesisi379 – 3791C → A or S: Loss of glutamine-dependent activity, but no change in ammonia-dependent activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 545544CTP synthasePRO_0000138183Add
BLAST

Proteomic databases

EPDiP0A7E5.
PaxDbiP0A7E5.
PRIDEiP0A7E5.

2D gel databases

SWISS-2DPAGEP0A7E5.

Interactioni

Subunit structurei

Homodimer in the absence of substrates and homotetramer in the presence of substrates with magnesium.

GO - Molecular functioni

  • identical protein binding Source: EcoCyc

Protein-protein interaction databases

DIPiDIP-10628N.
IntActiP0A7E5. 8 interactions.
STRINGi511145.b2780.

Structurei

Secondary structure

1
545
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 107Combined sources
Beta strandi12 – 143Combined sources
Helixi18 – 3013Combined sources
Turni31 – 333Combined sources
Beta strandi36 – 427Combined sources
Helixi49 – 513Combined sources
Turni54 – 563Combined sources
Beta strandi60 – 623Combined sources
Beta strandi68 – 703Combined sources
Helixi72 – 798Combined sources
Helixi86 – 883Combined sources
Beta strandi89 – 913Combined sources
Helixi92 – 10413Combined sources
Turni105 – 1106Combined sources
Helixi115 – 13117Combined sources
Beta strandi135 – 1417Combined sources
Helixi148 – 1503Combined sources
Helixi151 – 16414Combined sources
Beta strandi168 – 1769Combined sources
Turni181 – 1844Combined sources
Helixi189 – 19911Combined sources
Turni200 – 2023Combined sources
Beta strandi206 – 2149Combined sources
Helixi218 – 2269Combined sources
Helixi232 – 2343Combined sources
Beta strandi235 – 2395Combined sources
Helixi244 – 2463Combined sources
Helixi247 – 2537Combined sources
Helixi256 – 2638Combined sources
Helixi274 – 28411Combined sources
Beta strandi287 – 29812Combined sources
Helixi302 – 3054Combined sources
Helixi306 – 31813Combined sources
Beta strandi321 – 3299Combined sources
Helixi330 – 3367Combined sources
Turni338 – 3436Combined sources
Beta strandi345 – 3495Combined sources
Helixi358 – 37013Combined sources
Beta strandi375 – 3784Combined sources
Helixi380 – 39415Combined sources
Turni402 – 4043Combined sources
Beta strandi411 – 4144Combined sources
Turni416 – 4183Combined sources
Beta strandi440 – 4489Combined sources
Helixi453 – 4575Combined sources
Beta strandi460 – 46910Combined sources
Helixi475 – 4839Combined sources
Beta strandi487 – 4915Combined sources
Beta strandi493 – 4953Combined sources
Beta strandi498 – 5025Combined sources
Beta strandi506 – 5149Combined sources
Helixi516 – 5183Combined sources
Turni522 – 5243Combined sources
Helixi527 – 54216Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1MX-ray2.30A/B1-545[»]
2AD5X-ray2.80A/B1-545[»]
ProteinModelPortaliP0A7E5.
SMRiP0A7E5. Positions 1-545.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0A7E5.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini291 – 542252Glutamine amidotransferase type-1Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni2 – 253252Aminator domainAdd
BLAST

Sequence similaritiesi

Belongs to the CTP synthase family.Curated

Keywords - Domaini

Glutamine amidotransferase

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
InParanoidiP0A7E5.
KOiK01937.
OMAiMRLGEYE.
OrthoDBiEOG6RC3NR.
PhylomeDBiP0A7E5.

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.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0A7E5-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG
60 70 80 90 100
TMSPIQHGEV FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL
110 120 130 140 150
RKERRGDYLG ATVQVIPHIT NAIKERVLEG GEGHDVVLVE IGGTVGDIES
160 170 180 190 200
LPFLEAIRQM AVEIGREHTL FMHLTLVPYM AASGEVKTKP TQHSVKELLS
210 220 230 240 250
IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD VDSIYKIPGL
260 270 280 290 300
LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE
310 320 330 340 350
LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP
360 370 380 390 400
GGFGYRGVEG MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN
410 420 430 440 450
STEFVPDCKY PVVALITEWR DENGNVEVRS EKSDLGGTMR LGAQQCQLVD
460 470 480 490 500
DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ IEDAGLRVAG RSGDDQLVEI
510 520 530 540
IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ KRQAK
Length:545
Mass (Da):60,374
Last modified:January 23, 2007 - v2
Checksum:iFBB9E2E18FA355FC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti338 – 3381V → L in AAA24485 (PubMed:3514618).Curated
Sequence conflicti476 – 4761M → S in AAA24485 (PubMed:3514618).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12843 mRNA. Translation: AAA24485.1.
U29580 Genomic DNA. Translation: AAA69290.1.
U00096 Genomic DNA. Translation: AAC75822.1.
AP009048 Genomic DNA. Translation: BAE76854.1.
PIRiH65059. SYECTP.
RefSeqiNP_417260.1. NC_000913.3.
WP_000210878.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75822; AAC75822; b2780.
BAE76854; BAE76854; BAE76854.
GeneIDi946116.
KEGGiecj:JW2751.
eco:b2780.
PATRICi32120976. VBIEscCol129921_2880.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M12843 mRNA. Translation: AAA24485.1.
U29580 Genomic DNA. Translation: AAA69290.1.
U00096 Genomic DNA. Translation: AAC75822.1.
AP009048 Genomic DNA. Translation: BAE76854.1.
PIRiH65059. SYECTP.
RefSeqiNP_417260.1. NC_000913.3.
WP_000210878.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1S1MX-ray2.30A/B1-545[»]
2AD5X-ray2.80A/B1-545[»]
ProteinModelPortaliP0A7E5.
SMRiP0A7E5. Positions 1-545.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-10628N.
IntActiP0A7E5. 8 interactions.
STRINGi511145.b2780.

Protein family/group databases

MEROPSiC26.964.

2D gel databases

SWISS-2DPAGEP0A7E5.

Proteomic databases

EPDiP0A7E5.
PaxDbiP0A7E5.
PRIDEiP0A7E5.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75822; AAC75822; b2780.
BAE76854; BAE76854; BAE76854.
GeneIDi946116.
KEGGiecj:JW2751.
eco:b2780.
PATRICi32120976. VBIEscCol129921_2880.

Organism-specific databases

EchoBASEiEB0803.
EcoGeneiEG10810. pyrG.

Phylogenomic databases

eggNOGiENOG4105C8D. Bacteria.
COG0504. LUCA.
HOGENOMiHOG000077515.
InParanoidiP0A7E5.
KOiK01937.
OMAiMRLGEYE.
OrthoDBiEOG6RC3NR.
PhylomeDBiP0A7E5.

Enzyme and pathway databases

UniPathwayiUPA00159; UER00277.
BioCyciEcoCyc:CTPSYN-MONOMER.
ECOL316407:JW2751-MONOMER.
MetaCyc:CTPSYN-MONOMER.
BRENDAi6.3.4.2. 2026.

Miscellaneous databases

EvolutionaryTraceiP0A7E5.
PROiP0A7E5.

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

« Hide 'large scale' publications
  1. "Nucleotide sequence of Escherichia coli pyrG encoding CTP synthetase."
    Weng M., Makaroff C.A., Zalkin H.
    J. Biol. Chem. 261:5568-5574(1986) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / MG1655 / ATCC 47076.
  3. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
    Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
    Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
  4. "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12."
    Link A.J., Robison K., Church G.M.
    Electrophoresis 18:1259-1313(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-13.
    Strain: K12 / EMG2.
  5. "Structural role for a conserved region in the CTP synthetase glutamine amide transfer domain."
    Weng M., Zalkin H.
    J. Bacteriol. 169:3023-3028(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF VAL-349; GLY-351 AND GLY-352.
  6. "Characterization of metal ion activation and inhibition of CTP synthetase."
    Robertson J.G., Villafranca J.J.
    Biochemistry 32:3769-3777(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: ENZYME REGULATION.
  7. "Escherichia coli proteome analysis using the gene-protein database."
    VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.
    Electrophoresis 18:1243-1251(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY 2D-GEL.
  8. "Inhibition of Escherichia coli CTP synthase by glutamate gamma-semialdehyde and the role of the allosteric effector GTP in glutamine hydrolysis."
    Bearne S.L., Hekmat O., MacDonnell J.E.
    Biochem. J. 356:223-232(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: ROLE OF GTP, MUTAGENESIS OF CYS-379.

Entry informationi

Entry nameiPYRG_ECOLI
AccessioniPrimary (citable) accession number: P0A7E5
Secondary accession number(s): P08398, Q2MA52
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1988
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 102 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

GTP promotes glutamine amidotransferase activity, in part, by enhancing interactions between the enzyme and tetrahedral intermediate(s) formed during glutamine hydrolysis.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.