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Nomenclature

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Notes

Function

Gene Ontology
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Interactions See Help:Product_interactions for help entering or editing information about gene product interactions in this section of EcoliWiki.

Notes

Localization

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Notes

Structure and Physical Properties

Physical Properties See Help:Product_physical_properties for help entering or editing information about the physical properties of this gene product.

MPKRTDIKSI LILGAGPIVI GQACEFDYSG AQACKALREE GYRVILVNSN PATIMTDPEM
ADATYIEPIH WEVVRKIIEK ERPDAVLPTM GGQTALNCAL ELERQGVLEE FGVTMIGATA
DAIDKAEDRR RFDVAMKKIG LETARSGIAH TMEEALAVAA DVGFPCIIRP SFTMGGSGGG
IAYNREEFEE ICARGLDLSP TKELLIDESL IGWKEYEMEV VRDKNDNCII VCSIENFDAM
GIHTGDSITV APAQTLTDKE YQIMRNASMA VLREIGVETG GSNVQFAVNP KNGRLIVIEM
NPRVSRSSAL ASKATGFPIA KVAAKLAVGY TLDELMNDIT GGRTPASFEP SIDYVVTKIP
RFNFEKFAGA NDRLTTQMKS VGEVMAIGRT QQESLQKALR GLEVGATGFD PKVSLDDPEA
LTKIRRELKD AGADRIWYIA DAFRAGLSVD GVFNLTNIDR WFLVQIEELV RLEEKVAEVG
ITGLNADFLR QLKRKGFADA RLAKLAGVRE AEIRKLRDQY DLHPVYKRVD TCAAEFATDT
AYMYSTYEEE CEANPSTDRE KIMVLGGGPN RIGQGIEFDY CCVHASLALR EDGYETIMVN
CNPETVSTDY DTSDRLYFEP VTLEDVLEIV RIEKPKGVIV QYGGQTPLKL ARALEAAGVP
VIGTSPDAID RAEDRERFQH AVERLKLKQP ANATVTAIEM AVEKAKEIGY PLVVRPSYVL
GGRAMEIVYD EADLRRYFQT AVSVSNDAPV LLDHFLDDAV EVDVDAICDG EMVLIGGIME
HIEQAGVHSG DSACSLPAYT LSQEIQDVMR QQVQKLAFEL QVRGLMNVQF AVKNNEVYLI
EVNPRAARTV PFVSKATGVP LAKVAARVMA GKSLAEQGVT KEVIPPYYSV KEVVLPFNKF
PGVDPLLGPE MRSTGEVMGV GRTFAEAFAK AQLGSNSTMK KHGRALLSVR EGDKERVVDL
AAKLLKQGFE LDATHGTAIV LGEAGINPRL VNKVHEGRPH IQDRIKNGEY TYIINTTSGR
RAIEDSRVIR RSALQYKVHY DTTLNGGFAT AMALNADATE KVISVQEMHA QIK

See Help:Product_domains_motifs for help entering or editing information in this section of EcoliWiki. Type Residues Description Notes References Initiator Methionine 1 Removed UniProt:P00968 edit table

Notes

Gene Product Resources

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Notes

Accessions in Other Databases

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Notes

Links

References

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1. ↑ ^{1.0 1.1 1.2 1.3 1.4 1.5 1.6 1.7} Riley, M. et al. (2006) Nucleic Acids Res 34:1-6 (corrected supplemental data from B. Wanner)
2. ↑ ^{2.0 2.1 2.2 2.3 2.4 2.5 2.6 2.7} EcoCyc (release 10.6; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
3. ↑ ^{3.0 3.1} EcoCyc (release 11.1; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
4. ↑ EcoGene: Rudd, KE (2000) EcoGene: a genome sequence database for Escherichia coli K-12. Nucleic Acids Res 28:60-4.
5. ↑ ^{5.0 5.1 5.2 5.3 5.4} EcoCyc (release 13.0; 2009) Keseler, IM et al. (2009) Nucleic Acids Res. 37(Database issue):D464-70
6. ↑ ^{6.00 6.01 6.02 6.03 6.04 6.05 6.06 6.07 6.08 6.09 6.10} EcoCyc (release 12.5; 2007) Keseler, IM et al. (2005) Nucleic Acids Res. 33(Database issue):D334-7
7. ↑ Butland G et al. (2005) Interaction network containing conserved and essential protein complexes in Escherichia coli. Nature 433: 531-7 PubMed EcoliWiki page
8. ↑ ^{8.0 8.1 8.2} Kothe M & Powers-Lee SG (2004) Nucleotide recognition in the ATP-grasp protein carbamoyl phosphate synthetase. Protein Sci 13: 466-75 PubMed EcoliWiki page
9. ↑ ^{9.0 9.1} Trotta PP et al. (1974) Reversible dissociation of the monomer of glutamine-dependent carbamyl phosphate synthetase into catalytically active heavy and light subunits. J Biol Chem 249: 492-9 PubMed EcoliWiki page
10. ↑ Rubino SD et al. (1987) In vivo synthesis of carbamyl phosphate from NH3 by the large subunit of Escherichia coli carbamyl phosphate synthetase. J Biol Chem 262: 4382-6 PubMed EcoliWiki page
11. ↑ ^{11.0 11.1} Raushel FM et al. (1979) Paramagnetic probes for carbamoyl-phosphate synthetase: metal ion binding studies and preparation of nitroxide spin-labeled derivatives. Biochemistry 18: 5562-6 PubMed EcoliWiki page
12. ↑ ^{12.0 12.1 12.2} Guillou F et al. (1992) Mutational analysis of carbamyl phosphate synthetase. Substitution of Glu841 leads to loss of functional coupling between the two catalytic domains of the synthetase subunit. Biochemistry 31: 1656-64 PubMed EcoliWiki page
13. ↑ Fresquet V et al. (2000) Site-directed mutagenesis of the regulatory domain of Escherichia coli carbamoyl phosphate synthetase identifies crucial residues for allosteric regulation and for transduction of the regulatory signals. J Mol Biol 299: 979-91 PubMed EcoliWiki page
14. ↑ ^{14.0 14.1} Mareya SM & Raushel FM (1995) Mapping the structural domains of E. coli carbamoyl phosphate synthetase using limited proteolysis. Bioorg Med Chem 3: 525-32 PubMed EcoliWiki page
15. ↑ Thoden JB et al. (2004) Long-range allosteric transitions in carbamoyl phosphate synthetase. Protein Sci 13: 2398-405 PubMed EcoliWiki page
16. ↑ Delannay S et al. (1999) Serine 948 and threonine 1042 are crucial residues for allosteric regulation of Escherichia coli carbamoylphosphate synthetase and illustrate coupling effects of activation and inhibition pathways. J Mol Biol 286: 1217-28 PubMed EcoliWiki page
17. ↑ ^{17.0 17.1 17.2 17.3} Arifuzzaman M et al. (2006) Large-scale identification of protein-protein interaction of Escherichia coli K-12. Genome Res 16: 686-91 PubMed EcoliWiki page

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