Aspartate carbamoyltransferase regulatory chain (P0A7F3)

Identification
Name:Aspartate carbamoyltransferase regulatory chain
Synonyms:Not Available
Gene Name:pyrI
Enzyme Class:Not Available
Biological Properties
General Function:Involved in 'de novo' pyrimidine base biosynthetic process
Specific Function:Involved in allosteric regulation of aspartate carbamoyltransferase
Cellular Location:Not Available
SMPDB Pathways:
KEGG Pathways:
KEGG Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Carbamoylphosphate ↔ 1.0Ureidosuccinic acid + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb
1.0Carbamoylphosphate + 1.0L-Aspartic acid ↔ 1.0Phosphate + 1.0Ureidosuccinic acid
ReactionCard
SMPDB Reactions:
1.0L-Aspartic acid+1.0Thumb → 1.0Thumb
1.0L-Aspartic acid + 1.0L-Aspartic acid → 1.0N-carbamoyl-L-aspartate
ReactionCard
1.0Thumb+1.0L-Aspartic acid+1.0Thumb → 1.0Thumb+1.0Thumb+1.0Thumb
1.0Carbamoylphosphate + 1.0L-Aspartic acid + 1.0L-Aspartic acid → 1.0Phosphate + 1.0Hydrogen ion + 1.0N-carbamoyl-L-aspartate
ReactionCard
EcoCyc Reactions:
1.0Thumb+1.0Thumb ↔ 1.0Thumb+1.0Thumb+1.0Thumb
1.0L-Aspartic acid + 1.0Carbamoylphosphate ↔ 1.0Ureidosuccinic acid + 1.0Hydrogen ion + 1.0Phosphate
ReactionCard
Metabolites:
ECMDB IDNameView
ECMDB01096CarbamoylphosphateMetaboCard
ECMDB21225Hydrogen ionMetaboCard
ECMDB00191L-Aspartic acidMetaboCard
ECMDB24189N-carbamoyl-L-aspartateMetaboCard
ECMDB01429PhosphateMetaboCard
ECMDB00828Ureidosuccinic acidMetaboCard
GO Classification:
Component
aspartate carbamoyltransferase complex
macromolecular complex
protein complex
Process
'de novo' pyrimidine base biosynthetic 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:b4244
Gene OrientationCounterclockwise
Centisome Percentage:96.32
Left Sequence End4469009
Right Sequence End4469470
Gene Sequence:
>462 bp
GTGAGCAGAGTAACCGCGATTATATCCGCTCTGATTATCTGCATCATCGTCAGCCTGTCA
TGGGCGGTCAATCATTACCGTGATAACGCAATCGCCTACAAAGTCCAGCGCGACAAAAAT
GCCAGAGAACTGAAGCTAGCGAACGCGGCAATTACTGACATGCAGATGCGTCAGCGTGAT
GTTGCTGCGCTCGATGCAAAATACACGAAGGAGTTAGCTGATGCGAAAGCTGAAAATGAT
GCTCTGCGTGATGATGTTGCCGCTGGTCGTCGTCGGTTGCACATCAAAGCAGTCTGTCAG
TCAGTGCGTGAAGCCACCACGGCCTCCGGCGTGGATAATGCAGCCTCCCCCCGACTGGCA
GACACCGCTGAACGGGATTATTTCACCCTCAGAGAGAGGCTGATCACTATGCAAAAACAA
CTGGAAGGAACCCAGAAGTATATTAATGAGCAGTGCAGATAG
Protein Properties
Pfam Domain Function:
Protein Residues:153
Protein Molecular Weight:17121
Protein Theoretical pI:7
PDB File:1TUG
Signaling Regions:
  • None
Transmembrane Regions:
  • None
Protein Sequence:
>Aspartate carbamoyltransferase regulatory chain
MTHDNKLQVEAIKRGTVIDHIPAQIGFKLLSLFKLTETDQRITIGLNLPSGEMGRKDLIK
IENTFLSEDQVDQLALYAPQATVNRIDNYEVVGKSRPSLPERIDNVLVCPNSNCISHAEP
VSSSFAVRKRANDIALKCKYCEKEFSHNVVLAN
References
External Links:
ResourceLink
Uniprot ID:P0A7F3
Uniprot Name:PYRI_ECOLI
GenBank Gene ID:AP009048
Genebank Protein ID:85674691
PDB ID:1TUG
Ecogene ID:EG10811
Ecocyc:EG10811
ColiBase:b4244
Kegg Gene:b4244
EchoBASE ID:EB0804
CCDB:PYRI_ECOLI
BacMap:16132066
General Reference:
  • 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
  • Cunin, R., Jacobs, A., Charlier, D., Crabeel, M., Herve, G., Glansdorff, N., Pierard, A. (1985). "Structure-function relationship in allosteric aspartate carbamoyltransferase from Escherichia coli. I. Primary structure of a pyrI gene encoding a modified regulatory subunit." J Mol Biol 186:707-713. Pubmed: 3912513
  • 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
  • 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
  • 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
  • Monaco, H. L., Crawford, J. L., Lipscomb, W. N. (1978). "Three-dimensional structures of aspartate carbamoyltransferase from Escherichia coli and of its complex with cytidine triphosphate." Proc Natl Acad Sci U S A 75:5276-5280. Pubmed: 364472
  • 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
  • Weber, K. (1968). "New structural model of E. coli aspartate transcarbamylase and the amino-acid sequence of the regulatory polypeptide chain." Nature 218:1116-1119. Pubmed: 4872216