Aspartate carbamoyltransferase catalytic subunit
Details
- Name
- Aspartate carbamoyltransferase catalytic subunit
- Synonyms
- 2.1.3.2
- Aspartate transcarbamylase
- ATCase
- Gene Name
- pyrB
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0017068|Aspartate carbamoyltransferase catalytic subunit MANPLYQKHIISINDLSRDDLNLVLATAAKLKANPQPELLKHKVIASCFFEASTRTRLSF ETSMHRLGASVVGFSDSANTSLGKKGETLADTISVISTYVDAIVMRHPQEGAARLATEFS GNVPVLNAGDGSNQHPTQTLLDLFTIQETQGRLDNLHVAMVGDLKYGRTVHSLTQALAKF DGNRFYFIAPDALAMPQYILDMLDEKGIAWSLHSSIEEVMAEVDILYMTRVQKERLDPSE YANVKAQFVLRASDLHNAKANMKVLHPLPRVDEIATDVDKTPHAWYFQQAGNGIFARQAL LALVLNRDLVL
- Number of residues
- 311
- Molecular Weight
- 34427.02
- Theoretical pI
- 6.59
- GO Classification
- Functionsamino acid binding / aspartate carbamoyltransferase activityProcesses'de novo' pyrimidine nucleobase biosynthetic process / 'de novo' UMP biosynthetic process / cellular amino acid metabolic process / pyrimidine ribonucleotide biosynthetic processComponentscytoplasm / cytosol
- General Function
- Not Available
- Specific Function
- Amino acid binding
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0017069|Aspartate carbamoyltransferase catalytic subunit (pyrB) ATGGCTAATCCGCTATATCAGAAACATATCATTTCCATAAACGACCTTAGTCGCGATGAC CTTAATCTGGTGCTGGCGACAGCGGCGAAACTGAAAGCAAACCCGCAACCAGAGCTGTTG AAGCACAAAGTCATTGCCAGCTGTTTCTTCGAAGCCTCTACCCGTACCCGCCTCTCTTTC GAAACATCTATGCACCGCCTGGGGGCCAGCGTGGTGGGCTTCTCCGACAGCGCCAATACA TCACTGGGTAAAAAGGGCGAAACGCTGGCCGATACCATTTCGGTTATCAGCACTTACGTC GATGCGATAGTGATGCGTCATCCGCAGGAAGGTGCGGCGCGCCTGGCCACCGAGTTTTCC GGCAATGTACCGGTACTGAATGCCGGTGATGGCTCCAACCAACATCCGACGCAAACCTTG CTGGACTTATTCACTATTCAGGAAACCCAGGGGCGTCTGGACAATCTCCACGTCGCAATG GTTGGTGACCTGAAATATGGCCGCACCGTTCACTCCCTGACTCAGGCGTTAGCGAAGTTC GACGGCAACCGTTTTTACTTCATCGCGCCGGACGCGCTGGCAATGCCGCAATACATTCTG GATATGCTCGATGAAAAAGGGATCGCATGGAGTCTGCACAGCTCTATTGAAGAAGTGATG GCGGAAGTAGACATCCTGTACATGACCCGCGTGCAAAAAGAGCGTCTGGACCCGTCCGAG TACGCCAACGTGAAAGCGCAGTTTGTTCTTCGCGCCAGCGATCTCCACAACGCCAAAGCC AATATGAAAGTGCTGCATCCGCTGCCGCGTGTTGATGAGATTGCGACGGATGTTGATAAA ACGCCACACGCCTGGTACTTCCAGCAGGCAGGCAACGGGATTTTCGCTCGCCAGGCGTTA CTGGCACTGGTTCTGAATCGCGATCTGGTACTGTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P0A786 UniProtKB Entry Name PYRB_ECOLI GenBank Gene ID J01670 - General References
- Hoover TA, Roof WD, Foltermann KF, O'Donovan GA, Bencini DA, Wild JR: 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. 1983 May;80(9):2462-6. [Article]
- Schachman HK, Pauza CD, Navre M, Karels MJ, Wu L, Yang YR: Location of amino acid alterations in mutants of aspartate transcarbamoylase: Structural aspects of interallelic complementation. Proc Natl Acad Sci U S A. 1984 Jan;81(1):115-9. [Article]
- Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL, Blattner FR: Analysis of the Escherichia coli genome VI: DNA sequence of the region from 92.8 through 100 minutes. Nucleic Acids Res. 1995 Jun 25;23(12):2105-19. [Article]
- Blattner FR, Plunkett G 3rd, Bloch CA, Perna NT, Burland V, Riley M, Collado-Vides J, Glasner JD, Rode CK, Mayhew GF, Gregor J, Davis NW, Kirkpatrick HA, Goeden MA, Rose DJ, Mau B, Shao Y: The complete genome sequence of Escherichia coli K-12. Science. 1997 Sep 5;277(5331):1453-62. [Article]
- Hayashi K, Morooka N, Yamamoto Y, Fujita K, Isono K, Choi S, Ohtsubo E, Baba T, Wanner BL, Mori H, Horiuchi T: Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110. Mol Syst Biol. 2006;2:2006.0007. Epub 2006 Feb 21. [Article]
- Konigsberg WH, Henderson L: Amino acid sequence of the catalytic subunit of aspartate transcarbamoylase from Escherichia coli. Proc Natl Acad Sci U S A. 1983 May;80(9):2467-71. [Article]
- Roland KL, Liu CG, Turnbough CL Jr: Role of the ribosome in suppressing transcriptional termination at the pyrBI attenuator of Escherichia coli K-12. Proc Natl Acad Sci U S A. 1988 Oct;85(19):7149-53. [Article]
- Roland KL, Powell FE, Turnbough CL Jr: Role of translation and attenuation in the control of pyrBI operon expression in Escherichia coli K-12. J Bacteriol. 1985 Sep;163(3):991-9. [Article]
- Turnbough CL Jr, Hicks KL, Donahue JP: Attenuation control of pyrBI operon expression in Escherichia coli K-12. Proc Natl Acad Sci U S A. 1983 Jan;80(2):368-72. [Article]
- Donahue JP, Turnbough CL Jr: Characterization of transcriptional initiation from promoters P1 and P2 of the pyrBI operon of Escherichia coli K12. J Biol Chem. 1990 Nov 5;265(31):19091-9. [Article]
- Link AJ, Robison K, Church GM: Comparing the predicted and observed properties of proteins encoded in the genome of Escherichia coli K-12. Electrophoresis. 1997 Aug;18(8):1259-313. [Article]
- Molloy MP, Herbert BR, Walsh BJ, Tyler MI, Traini M, Sanchez JC, Hochstrasser DF, Williams KL, Gooley AA: Extraction of membrane proteins by differential solubilization for separation using two-dimensional gel electrophoresis. Electrophoresis. 1998 May;19(5):837-44. [Article]
- VanBogelen RA, Abshire KZ, Moldover B, Olson ER, Neidhardt FC: Escherichia coli proteome analysis using the gene-protein database. Electrophoresis. 1997 Aug;18(8):1243-51. [Article]
- Ke HM, Honzatko RB, Lipscomb WN: Structure of unligated aspartate carbamoyltransferase of Escherichia coli at 2.6-A resolution. Proc Natl Acad Sci U S A. 1984 Jul;81(13):4037-40. [Article]
- Stevens RC, Gouaux JE, Lipscomb WN: 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. 1990 Aug 21;29(33):7691-701. [Article]
- Gouaux JE, Stevens RC, Lipscomb WN: Crystal structures of aspartate carbamoyltransferase ligated with phosphonoacetamide, malonate, and CTP or ATP at 2.8-A resolution and neutral pH. Biochemistry. 1990 Aug 21;29(33):7702-15. [Article]
- Beernink PT, Endrizzi JA, Alber T, Schachman HK: 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. 1999 May 11;96(10):5388-93. [Article]