Identification
Name:Aspartate carbamoyltransferase catalytic chain
Synonyms:
  • Aspartate transcarbamylase
  • ATCase
Gene Name:pyrB
Enzyme Class:
Biological Properties
General Function:Involved in carboxyl- or carbamoyltransferase activity
Specific Function:Carbamoyl phosphate + L-aspartate = phosphate + N-carbamoyl-L-aspartate
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
SMPDB Reactions:
1.0L-Aspartic acid+1.0Thumb1.0Thumb
1.0Thumb+1.0L-Aspartic acid+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
EcoCyc Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb+1.0Thumb
Complex Reactions:
1.0Thumb+1.0Thumb1.0Thumb+1.0Thumb
Metabolites:
ECMDB IDNameView
ECMDB01096CarbamoylphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB21380Inorganic phosphateMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB24189N-carbamoyl-L-aspartateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00828Ureidosuccinic acidMetaboCard
GO Classification:
Function
amino acid binding
aspartate carbamoyltransferase activity
binding
carboxyl- or carbamoyltransferase activity
carboxylic acid binding
catalytic activity
transferase activity
transferase activity, transferring one-carbon groups
Process
'de novo' pyrimidine base biosynthetic process
cellular amino acid and derivative metabolic process
cellular amino acid metabolic process
cellular aromatic compound metabolic process
cellular metabolic process
metabolic process
nucleobase metabolic process
pyrimidine base biosynthetic process
pyrimidine base metabolic process
Gene Properties
Blattner:b4245
Gene OrientationCounterclockwise
Centisome Percentage:96.33
Left Sequence End4469483
Right Sequence End4470418
Gene Sequence:
>936 bp
ATGGCCGCCGTTAACTTACGTCATATTGAAATTTTTCATGCGGTAATGACCGCCGGAAGC
CTGACTGAGGCGGCACACCTGCTACACACCTCACAGCCAACCGTCAGCCGCGAACTTGCG
CGCTTTGAGAAGGTGATCGGGCTGAAATTGTTTGAGCGCGTACGTGGGCGATTACATCCT
ACCGTGCAAGGACTGCGTCTGTTTGAAGAAGTGCAACGATCCTGGTACGGACTGGATCGC
ATTGTCAGCGCCGCAGAAAGTCTGCGCGAGTTTCGCCAGGGAGAACTGTCTATTGCCTGC
CTGCCGGTCTTTTCGCAATCTTTTTTACCGCAGCTCCTGCAACCCTTTCTGGCACGTTAT
CCCGATGTCAGCTTAAATATCGTGCCCCAGGAATCACCGCTACTTGAAGAGTGGCTCTCG
GCCCAGCGTCATGATTTAGGACTCACTGAAACGCTCCATACGCCTGCGGGAACAGAACGT
ACCGAATTACTCTCTTTAGATGAAGTGTGTGTGTTACCTCCGGGTCATCCGCTGGCGGTA
AAAAAGGTATTAACGCCGGATGATTTTCAGGGTGAGAACTACATCAGCCTTTCCCGTACT
GACAGCTATCGCCAGTTGCTGGATCAGCTATTTACTGAACATCAGGTTAAACGACGCATG
ATCGTAGAAACCCACAGCGCCGCGTCAGTCTGCGCAATGGTACGGGCGGGGGTAGGTATT
TCGGTGGTTAACCCGCTCACCGCACTAGATTATGCGGCAAGCGGTTTAGTGGTGCGGCGG
TTCAGTATTGCGGTTCCGTTCACCGTCAGCCTGATCCGCCCCCTGCACCGCCCGTCATCA
GCGCTGGTTCAGGCGTTTAGTGGGCATTTACAAGCGGGGTTACCGAAACTGGTCACTTCT
CTTGACGCTATTTTGTCGTCAGCTACGACAGCATAA
Protein Properties
Pfam Domain Function:
Protein Residues:311
Protein Molecular Weight:34427
Protein Theoretical pI:7
PDB File:1EKX
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartate carbamoyltransferase catalytic chain
MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSF
ETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFS
GNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKF
DGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSE
YANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQAL
LALVLNRDLVL
References
External Links:
ResourceLink
Uniprot ID:P0A786
Uniprot Name:PYRB_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85675655
PDB ID:1EKX
Ecogene ID:EG10805
Ecocyc:EG10805
ColiBase:b4245
Kegg Gene:b4245
EchoBASE ID:EB0798
CCDB:PYRB_ECOLI
BacMap:16132067
General Reference:
  • Beernink, P. T., Endrizzi, J. A., Alber, T., Schachman, H. K. (1999). "Assessment of the allosteric mechanism of aspartate transcarbamoylase based on the crystalline structure of the unregulated catalytic subunit." Proc Natl Acad Sci U S A 96:5388-5393. Pubmed: 10318893
  • Blattner, F. R., Plunkett, G. 3rd, Bloch, C. A., Perna, N. T., Burland, V., Riley, M., Collado-Vides, J., Glasner, J. D., Rode, C. K., Mayhew, G. F., Gregor, J., Davis, N. W., Kirkpatrick, H. A., Goeden, M. A., Rose, D. J., Mau, B., Shao, Y. (1997). "The complete genome sequence of Escherichia coli K-12." Science 277:1453-1462. Pubmed: 9278503
  • Burland, V., Plunkett, G. 3rd, Sofia, H. J., Daniels, D. L., Blattner, F. R. (1995). "Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes." Nucleic Acids Res 23:2105-2119. Pubmed: 7610040
  • Donahue, J. P., Turnbough, C. L. Jr (1990). "Characterization of transcriptional initiation from promoters P1 and P2 of the pyrBI operon of Escherichia coli K12." J Biol Chem 265:19091-19099. Pubmed: 1699940
  • Gouaux, J. E., Stevens, R. C., Lipscomb, W. N. (1990). "Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH." Biochemistry 29:7702-7715. Pubmed: 2271529
  • Hayashi, K., Morooka, N., Yamamoto, Y., Fujita, K., Isono, K., Choi, S., Ohtsubo, E., Baba, T., Wanner, B. L., Mori, H., Horiuchi, T. (2006). "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Mol Syst Biol 2:2006.0007. Pubmed: 16738553
  • Hoover, T. A., Roof, W. D., Foltermann, K. F., O'Donovan, G. A., Bencini, D. A., Wild, J. R. (1983). "Nucleotide sequence of the structural gene (pyrB) that encodes the catalytic polypeptide of aspartate transcarbamoylase of Escherichia coli." Proc Natl Acad Sci U S A 80:2462-2466. Pubmed: 6302686
  • Ke, H. M., Honzatko, R. B., Lipscomb, W. N. (1984). "Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution." Proc Natl Acad Sci U S A 81:4037-4040. Pubmed: 6377306
  • Konigsberg, W. H., Henderson, L. (1983). "Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli." Proc Natl Acad Sci U S A 80:2467-2471. Pubmed: 6341995
  • Link, A. J., Robison, K., Church, G. M. (1997). "Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12." Electrophoresis 18:1259-1313. Pubmed: 9298646
  • Molloy, M. P., Herbert, B. R., Walsh, B. J., Tyler, M. I., Traini, M., Sanchez, J. C., Hochstrasser, D. F., Williams, K. L., Gooley, A. A. (1998). "Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis." Electrophoresis 19:837-844. Pubmed: 9629924
  • Roland, K. L., Liu, C. G., Turnbough, C. L. Jr (1988). "Role of the ribosome in suppressing transcriptional termination at the pyrBI attenuator of Escherichia coli K-12." Proc Natl Acad Sci U S A 85:7149-7153. Pubmed: 2459698
  • Roland, K. L., Powell, F. E., Turnbough, C. L. Jr (1985). "Role of translation and attenuation in the control of pyrBI operon expression in Escherichia coli K-12." J Bacteriol 163:991-999. Pubmed: 3928602
  • Schachman, H. K., Pauza, C. D., Navre, M., Karels, M. J., Wu, L., Yang, Y. R. (1984). "Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation." Proc Natl Acad Sci U S A 81:115-119. Pubmed: 6364131
  • Stevens, R. C., Gouaux, J. E., Lipscomb, W. N. (1990). "Structural consequences of effector binding to the T state of aspartate carbamoyltransferase: crystal structures of the unligated and ATP- and CTP-complexed enzymes at 2.6-A resolution." Biochemistry 29:7691-7701. Pubmed: 2271528
  • Turnbough, C. L. Jr, Hicks, K. L., Donahue, J. P. (1983). "Attenuation control of pyrBI operon expression in Escherichia coli K-12." Proc Natl Acad Sci U S A 80:368-372. Pubmed: 6300835