pyrG:Gene Product(s)
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Quickview | Gene | Gene Product(s) | Expression | Evolution | On One Page |
Nomenclature | Function | Interactions | Localization | Sequence | Domains | Structure | Resources | Accessions | Links | References | Suggestions |
Nomenclature
See Help:Product_nomenclature for help entering or editing information in this section of EcoliWiki.
Standard name |
PyrG |
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Synonyms |
CTP synthetase[1], B2780[2][1], PyrG[2][1] , ECK2774, JW2751, b2780 |
Product description |
Component of CTP synthetase[2][3] CTP synthase[4] |
EC number (for enzymes) | |
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Notes
Catalyzes the reaction:
ATP + UTP + L-glutamine + H2O -> ADP + phosphate + CTP + L-glutamate[1]
Note that the reaction is irreversible in the direction shown.
Function
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Gene Ontology
See Help:Gene_ontology for help entering or editing GO terms and GO annotations in EcoliWiki.
Qualifier | GO ID | GO term name | Reference | Evidence Code | with/from | Aspect | Notes | Status |
---|---|---|---|---|---|---|---|---|
GO:0005737 |
cytoplasm |
C |
Seeded from Riley et al 2006 [1]. |
Missing: evidence, reference | ||||
GO:0000166 |
nucleotide binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003883 |
CTP synthase activity |
GOA:hamap |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003883 |
CTP synthase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003883 |
CTP synthase activity |
IDA: Inferred from Direct Assay |
F |
Showed that glutamine rather than NH3 is the primary amino donor. |
complete | |||
GO:0003883 |
CTP synthase activity |
GOA:interpro |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0003883 |
CTP synthase activity |
GOA:spec |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005524 |
ATP binding |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
F |
Seeded from EcoCyc (v14.0) |
complete | ||
GO:0005829 |
cytosol |
IDA: Inferred from Direct Assay |
C |
Seeded from EcoCyc (v14.0) |
complete | |||
GO:0006541 |
glutamine metabolic process |
GOA:spkw |
IEA: Inferred from Electronic Annotation |
P |
Seeded from EcoCyc (v14.0) |
complete | ||
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.
Partner Type | Partner | Notes | References | Evidence |
---|---|---|---|---|
Protein |
Subunits of CTP synthetase |
could be indirect |
||
Protein |
rpoB |
Experiment(s):EBI-1143918 | ||
Protein |
ybfF |
Experiment(s):EBI-1143918 | ||
Protein |
hsdR |
Experiment(s):EBI-1143918 | ||
Protein |
rpoC |
Experiment(s):EBI-1143918 | ||
Protein |
hchA |
Experiment(s):EBI-1143918 | ||
Protein |
nadE |
Experiment(s):EBI-1143918 | ||
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Notes
Localization
See Help:Product_localization for how to add or edit information in this section of EcoliWiki.
Compartment | Description | Evidence | Reference/Source | Notes |
---|---|---|---|---|
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Notes
Structure and Physical Properties
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Physical Properties
See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.
Name | |
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Sequence |
MTTNYIFVTG GVVSSLGKGI AAASLAAILE ARGLNVTIMK LDPYINVDPG TMSPIQHGEV FVTEDGAETD LDLGHYERFI RTKMSRRNNF TTGRIYSDVL RKERRGDYLG ATVQVIPHIT NAIKERVLEG GEGHDVVLVE IGGTVGDIES LPFLEAIRQM AVEIGREHTL FMHLTLVPYM AASGEVKTKP TQHSVKELLS IGIQPDILIC RSDRAVPANE RAKIALFCNV PEKAVISLKD VDSIYKIPGL LKSQGLDDYI CKRFSLNCPE ANLSEWEQVI FEEANPVSEV TIGMVGKYIE LPDAYKSVIE ALKHGGLKNR VSVNIKLIDS QDVETRGVEI LKGLDAILVP GGFGYRGVEG MITTARFARE NNIPYLGICL GMQVALIDYA RHVANMENAN STEFVPDCKY PVVALITEWR DENGNVEVRS EKSDLGGTMR LGAQQCQLVD DSLVRQLYNA PTIVERHRHR YEVNNMLLKQ IEDAGLRVAG RSGDDQLVEI IEVPNHPWFV ACQFHPEFTS TPRDGHPLFA GFVKAASEFQ KRQAK |
Length |
545 |
Mol. Wt |
60.374 kDa |
pI |
5.8 (calculated) |
Extinction coefficient |
40,340 - 41,340 (calc based on 16 Y, 3 W, and 8 C residues) |
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Domains/Motifs/Modification Sites
See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki.
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Structure
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Structure figures<protect> | ||||||
Notes
Gene Product Resources
See Help:Product_resources for help with entering or editing information in this section of EcoliWiki.
Resource type | Source | Notes/Reference |
---|---|---|
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Notes
Accessions in Other Databases
See Help:Gene_accessions for help with entering information into the Gene Accessions table.
Database | Accession | Notes |
---|---|---|
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
Escherichia coli str. K-12 substr. MG1655 | ||
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Notes
Links
Name | URL | Comments |
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References
See Help:References for how to manage references in EcoliWiki.
- ↑ 1.0 1.1 1.2 1.3 1.4 Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
- ↑ 2.0 2.1 2.2 2.3 EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ 3.0 3.1 EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
- ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
- ↑ CHAKRABORTY, KP & HURLBERT, RB (1961) Role of glutamine in the biosynthesis of cytidine nucleotides in Escherichia coli. Biochim. Biophys. Acta 47 607-9 PubMed
- ↑ Lasserre, JP et al. (2006) A complexomic study of Escherichia coli using two-dimensional blue native/SDS polyacrylamide gel electrophoresis. Electrophoresis 27 3306-21 PubMed
- ↑ 7.0 7.1 7.2 7.3 7.4 7.5 Arifuzzaman, M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res. 16 686-91 PubMed
- ↑ 8.0 8.1 Finn, RD et al. (2010) The Pfam protein families database. Nucleic Acids Res. 38 D211-22 PubMed
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