Phosphoenolpyruvate carboxylase
Details
- Name
- Phosphoenolpyruvate carboxylase
- Synonyms
- 4.1.1.31
- glu
- PEPC
- Gene Name
- ppc
- Organism
- Escherichia coli (strain K12)
- Amino acid sequence
>lcl|BSEQ0016578|Phosphoenolpyruvate carboxylase MNEQYSALRSNVSMLGKVLGETIKDALGEHILERVETIRKLSKSSRAGNDANRQELLTTL QNLSNDELLPVARAFSQFLNLANTAEQYHSISPKGEAASNPEVIARTLRKLKNQPELSED TIKKAVESLSLELVLTAHPTEITRRTLIHKMVEVNACLKQLDNKDIADYEHNQLMRRLRQ LIAQSWHTDEIRKLRPSPVDEAKWGFAVVENSLWQGVPNYLRELNEQLEENLGYKLPVEF VPVRFTSWMGGDRDGNPNVTADITRHVLLLSRWKATDLFLKDIQVLVSELSMVEATPELL ALVGEEGAAEPYRYLMKNLRSRLMATQAWLEARLKGEELPKPEGLLTQNEELWEPLYACY QSLQACGMGIIANGDLLDTLRRVKCFGVPLVRIDIRQESTRHTEALGELTRYLGIGDYES WSEADKQAFLIRELNSKRPLLPRNWQPSAETREVLDTCQVIAEAPQGSIAAYVISMAKTP SDVLAVHLLLKEAGIGFAMPVAPLFETLDDLNNANDVMTQLLNIDWYRGLIQGKQMVMIG YSDSAKDAGVMAASWAQYQAQDALIKTCEKAGIELTLFHGRGGSIGRGGAPAHAALLSQP PGSLKGGLRVTEQGEMIRFKYGLPEITVSSLSLYTGAILEANLLPPPEPKESWRRIMDEL SVISCDVYRGYVRENKDFVPYFRSATPEQELGKLPLGSRPAKRRPTGGVESLRAIPWIFA WTQNRLMLPAWLGAGTALQKVVEDGKQSELEAMCRDWPFFSTRLGMLEMVFAKADLWLAE YYDQRLVDKALWPLGKELRNLQEEDIKVVLAIANDSHLMADLPWIAESIQLRNIYTDPLN VLQAELLHRSRQAEKEGQEPDPRVEQALMVTIAGIAAGMRNTG
- Number of residues
- 883
- Molecular Weight
- 99061.63
- Theoretical pI
- 5.4
- GO Classification
- Functionsmagnesium ion binding / phosphoenolpyruvate carboxylase activityProcessescarbon fixation / oxaloacetate metabolic process / tricarboxylic acid cycleComponentscytosol
- General Function
- Phosphoenolpyruvate carboxylase activity
- Specific Function
- Forms oxaloacetate, a four-carbon dicarboxylic acid source for the tricarboxylic acid cycle.
- Pfam Domain Function
- PEPcase (PF00311)
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0016579|Phosphoenolpyruvate carboxylase (ppc) ATGAACGAACAATATTCCGCATTGCGTAGTAATGTCAGTATGCTCGGCAAAGTGCTGGGA GAAACCATCAAGGATGCGTTGGGAGAACACATTCTTGAACGCGTAGAAACTATCCGTAAG TTGTCGAAATCTTCACGCGCTGGCAATGATGCTAACCGCCAGGAGTTGCTCACCACCTTA CAAAATTTGTCGAACGACGAGCTGCTGCCCGTTGCGCGTGCGTTTAGTCAGTTCCTGAAC CTGGCCAACACCGCCGAGCAATACCACAGCATTTCGCCGAAAGGCGAAGCTGCCAGCAAC CCGGAAGTGATCGCCCGCACCCTGCGTAAACTGAAAAACCAGCCGGAACTGAGCGAAGAC ACCATCAAAAAAGCAGTGGAATCGCTGTCGCTGGAACTGGTCCTCACGGCTCACCCAACC GAAATTACCCGTCGTACACTGATCCACAAAATGGTGGAAGTGAACGCCTGTTTAAAACAG CTCGATAACAAAGATATCGCTGACTACGAACACAACCAGCTGATGCGTCGCCTGCGCCAG TTGATCGCCCAGTCATGGCATACCGATGAAATCCGTAAGCTGCGTCCAAGCCCGGTAGAT GAAGCCAAATGGGGCTTTGCCGTAGTGGAAAACAGCCTGTGGCAAGGCGTACCAAATTAC CTGCGCGAACTGAACGAACAACTGGAAGAGAACCTCGGCTACAAACTGCCCGTCGAATTT GTTCCGGTCCGTTTTACTTCGTGGATGGGCGGCGACCGCGACGGCAACCCGAACGTCACT GCCGATATCACCCGCCACGTCCTGCTACTCAGCCGCTGGAAAGCCACCGATTTGTTCCTG AAAGATATTCAGGTGCTGGTTTCTGAACTGTCGATGGTTGAAGCGACCCCTGAACTGCTG GCGCTGGTTGGCGAAGAAGGTGCCGCAGAACCGTATCGCTATCTGATGAAAAACCTGCGT TCTCGCCTGATGGCGACACAGGCATGGCTGGAAGCGCGCCTGAAAGGCGAAGAACTGCCA AAACCAGAAGGCCTGCTGACACAAAACGAAGAACTGTGGGAACCGCTCTACGCTTGCTAC CAGTCACTTCAGGCGTGTGGCATGGGTATTATCGCCAACGGCGATCTGCTCGACACCCTG CGCCGCGTGAAATGTTTCGGCGTACCGCTGGTCCGTATTGATATCCGTCAGGAGAGCACG CGTCATACCGAAGCGCTGGGCGAGCTGACCCGCTACCTCGGTATCGGCGACTACGAAAGC TGGTCAGAGGCCGACAAACAGGCGTTCCTGATCCGCGAACTGAACTCCAAACGTCCGCTT CTGCCGCGCAACTGGCAACCAAGCGCCGAAACGCGCGAAGTGCTCGATACCTGCCAGGTG ATTGCCGAAGCACCGCAAGGCTCCATTGCCGCCTACGTGATCTCGATGGCGAAAACGCCG TCCGACGTACTGGCTGTCCACCTGCTGCTGAAAGAAGCGGGTATCGGGTTTGCGATGCCG GTTGCTCCGCTGTTTGAAACCCTCGATGATCTGAACAACGCCAACGATGTCATGACCCAG CTGCTCAATATTGACTGGTATCGTGGCCTGATTCAGGGCAAACAGATGGTGATGATTGGC TATTCCGACTCAGCAAAAGATGCGGGAGTGATGGCAGCTTCCTGGGCGCAATATCAGGCA CAGGATGCATTAATCAAAACCTGCGAAAAAGCGGGTATTGAGCTGACGTTGTTCCACGGT CGCGGCGGTTCCATTGGTCGCGGCGGCGCACCTGCTCATGCGGCGCTGCTGTCACAACCG CCAGGAAGCCTGAAAGGCGGCCTGCGCGTAACCGAACAGGGCGAGATGATCCGCTTTAAA TATGGTCTGCCAGAAATCACCGTCAGCAGCCTGTCGCTTTATACCGGGGCGATTCTGGAA GCCAACCTGCTGCCACCGCCGGAGCCGAAAGAGAGCTGGCGTCGCATTATGGATGAACTG TCAGTCATCTCCTGCGATGTCTACCGCGGCTACGTACGTGAAAACAAAGATTTTGTGCCT TACTTCCGCTCCGCTACGCCGGAACAAGAACTGGGCAAACTGCCGTTGGGTTCACGTCCG GCGAAACGTCGCCCAACCGGCGGCGTCGAGTCACTACGCGCCATTCCGTGGATCTTCGCC TGGACGCAAAACCGTCTGATGCTCCCCGCCTGGCTGGGTGCAGGTACGGCGCTGCAAAAA GTGGTCGAAGACGGCAAACAGAGCGAGCTGGAGGCTATGTGCCGCGATTGGCCATTCTTC TCGACGCGTCTCGGCATGCTGGAGATGGTCTTCGCCAAAGCAGACCTGTGGCTGGCGGAA TACTATGACCAACGCCTGGTAGACAAAGCACTGTGGCCGTTAGGTAAAGAGTTACGCAAC CTGCAAGAAGAAGACATCAAAGTGGTGCTGGCGATTGCCAACGATTCCCATCTGATGGCC GATCTGCCGTGGATTGCAGAGTCTATTCAGCTACGGAATATTTACACCGACCCGCTGAAC GTATTGCAGGCCGAGTTGCTGCACCGCTCCCGCCAGGCAGAAAAAGAAGGCCAGGAACCG GATCCTCGCGTCGAACAAGCGTTAATGGTCACTATTGCCGGGATTGCGGCAGGTATGCGT AATACCGGCTAA
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P00864 UniProtKB Entry Name CAPP_ECOLI GenBank Protein ID 48666 GenBank Gene ID X05903 - General References
- Fujita N, Miwa T, Ishijima S, Izui K, Katsuki H: The primary structure of phosphoenolpyruvate carboxylase of Escherichia coli. Nucleotide sequence of the ppc gene and deduced amino acid sequence. J Biochem. 1984 Apr;95(4):909-16. [Article]
- Blattner FR, Burland V, Plunkett G 3rd, Sofia HJ, Daniels DL: Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes. Nucleic Acids Res. 1993 Nov 25;21(23):5408-17. [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]
- Meinnel T, Schmitt E, Mechulam Y, Blanquet S: Structural and biochemical characterization of the Escherichia coli argE gene product. J Bacteriol. 1992 Apr;174(7):2323-31. [Article]
- Izui K, Miwa T, Kajitani M, Fujita N, Sabe H, Ishihama A, Katsuki H: Promoter analysis of the phosphoenolpyruvate carboxylase gene of Escherichia coli. Nucleic Acids Res. 1985 Jan 11;13(1):59-71. [Article]
- Terada K, Murata T, Izui K: Site-directed mutagenesis of phosphoenolpyruvate carboxylase from E. coli: the role of His579 in the catalytic and regulatory functions. J Biochem. 1991 Jan;109(1):49-54. [Article]
- Terada K, Izui K: Site-directed mutagenesis of the conserved histidine residue of phosphoenolpyruvate carboxylase. His138 is essential for the second partial reaction. Eur J Biochem. 1991 Dec 18;202(3):797-803. [Article]
- Yano M, Terada K, Umiji K, Izui K: Catalytic role of an arginine residue in the highly conserved and unique sequence of phosphoenolpyruvate carboxylase. J Biochem. 1995 Jun;117(6):1196-200. [Article]
- Inoue M, Hayashi M, Sugimoto M, Harada S, Kai Y, Kasai N, Terada K, Izui K: First crystallization of a phosphoenolpyruvate carboxylase from Escherichia coli. J Mol Biol. 1989 Aug 5;208(3):509-10. [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]
- Kai Y, Matsumura H, Inoue T, Terada K, Nagara Y, Yoshinaga T, Kihara A, Tsumura K, Izui K: Three-dimensional structure of phosphoenolpyruvate carboxylase: a proposed mechanism for allosteric inhibition. Proc Natl Acad Sci U S A. 1999 Feb 2;96(3):823-8. [Article]