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Escherichia coli K-12 substr. MG1655 Enzyme: N-acetylglutamylphosphate reductase



Gene: argC Accession Numbers: EG10065 (EcoCyc), b3958, ECK3949

Synonyms: Arg2

Regulation Summary Diagram: ?

Summary:
N-acetylglutamylphosphate reductase (ArgC) carries out the third step in arginine biosynthesis and its subpathway, ornithine biosynthesis.

ArgC catalyzes the NADPH-dependent reduction of N-acetylglutamyl-phosphate to yield N-acetyl-L-glutamate 5-semialdehyde [Baich62, Parsot88, Vogel74].

Gene Citations: [Natter77, Sens77]

Locations: cytosol

Map Position: [4,153,024 -> 4,154,028] (89.51 centisomes)
Length: 1005 bp / 334 aa

Molecular Weight of Polypeptide: 35.952 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0012964 , CGSC:1019 , EchoBASE:EB0063 , EcoGene:EG10065 , EcoliWiki:b3958 , Entrez-gene:948455 , ModBase:P11446 , OU-Microarray:b3958 , PortEco:argC , Protein Model Portal:P11446 , RefSeq:NP_418393 , RegulonDB:EG10065 , SMR:P11446 , String:511145.b3958 , Swiss-Model:P11446 , UniProt:P11446

Relationship Links: InterPro:IN-FAMILY:IPR000534 , InterPro:IN-FAMILY:IPR000706 , InterPro:IN-FAMILY:IPR012280 , InterPro:IN-FAMILY:IPR016040 , InterPro:IN-FAMILY:IPR023013 , Pfam:IN-FAMILY:PF01118 , Pfam:IN-FAMILY:PF02774 , Prosite:IN-FAMILY:PS01224 , Smart:IN-FAMILY:SM00859

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006526 - arginine biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA12, UniProtGOA11a, GOA06, GOA01a, Takahara07, Baich62]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
Molecular Function: GO:0003942 - N-acetyl-gamma-glutamyl-phosphate reductase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Baich62]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a]
GO:0016620 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01a]
GO:0046983 - protein dimerization activity Inferred by computational analysis [GOA01a]
GO:0051287 - NAD binding Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06, GOA01a]
GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids arginine

Essentiality data for argC knockouts: ?

Growth Medium Growth? T (°C) O2 pH Osm/L Growth Observations
LB Lennox Yes 37 Aerobic 7   Yes [Baba06, Comment 1]
M9 medium with 0.4% glucose No 37 Aerobic 7.2 0.27 No [Patrick07, Comment 2]
M9 medium with 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 3]
MOPS medium with 0.4% glucose Indeterminate 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
No [Feist07, Comment 4]

Credits:
Last-Curated ? 09-Nov-2007 by Shearer A , SRI International


Enzymatic reaction of: N-acetylglutamylphosphate reductase

Synonyms: N-acetyl-glutamate semialdehyde dehydrogenase, NAGSA dehydrogenase, N-acetyl-γ-glutamyl-phosphate reductase, N-acetyl-Lglutamate-5-semialdehyde:NADP+ 5-oxidoreductase (phosphorylating)

EC Number: 1.2.1.38

N-acetyl-L-glutamate 5-semialdehyde + NADP+ + phosphate <=> N-acetylglutamyl-phosphate + NADPH + H+

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the direction of enzyme catalysis.

This reaction is reversible. [Takahara07]

In Pathways: superpathway of arginine and polyamine biosynthesis , arginine biosynthesis I (via L-ornithine) , ornithine biosynthesis

Summary:
This reaction can use arsenate in place of phosphate [Vogel74].

In general, inhibition of this reaction is more effective in the presence of phosphate [Vogel74].

Inhibitors (Unknown Mechanism): a sulfhydryl reagent [Vogel74] , Fe2+ [Vogel74] , Mn2+ [Vogel74] , Ni2+ [Vogel74] , Cu2+ [Vogel74] , Zn2+ [Vogel74]

Kinetic Parameters:

Substrate
Km (μM)
Citations
phosphate
3000.0
[WandingerNess86, BRENDA14]

pH(opt): 9.3 [BRENDA14, WandingerNess86]


Sequence Features

Feature Class Location Citations Comment
Active-Site 154
[UniProt10]
UniProt: Non-Experimental Qualifier: by similarity;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
10/20/97 Gene b3958 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10065; confirmed by SwissProt match.


References

Baba06: Baba T, Ara T, Hasegawa M, Takai Y, Okumura Y, Baba M, Datsenko KA, Tomita M, Wanner BL, Mori H (2006). "Construction of Escherichia coli K-12 in-frame, single-gene knockout mutants: the Keio collection." Mol Syst Biol 2;2006.0008. PMID: 16738554

Baich62: Baich A, Vogel HJ (1962). "N-Acetyl-gamma-Ilutamokinase and N-acetylglutamic gamma-semialdehyde dehydrogenase: repressible enzymes of arginine synthesis in Escherichia coli." Biochem Biophys Res Commun 7;491-6. PMID: 13863980

BRENDA14: BRENDA team (2014). "Imported from BRENDA version existing on Aug 2014." http://www.brenda-enzymes.org.

DiazMejia09: Diaz-Mejia JJ, Babu M, Emili A (2009). "Computational and experimental approaches to chart the Escherichia coli cell-envelope-associated proteome and interactome." FEMS Microbiol Rev 33(1);66-97. PMID: 19054114

Feist07: Feist AM, Henry CS, Reed JL, Krummenacker M, Joyce AR, Karp PD, Broadbelt LJ, Hatzimanikatis V, Palsson BO (2007). "A genome-scale metabolic reconstruction for Escherichia coli K-12 MG1655 that accounts for 1260 ORFs and thermodynamic information." Mol Syst Biol 3;121. PMID: 17593909

GOA01: GOA, MGI (2001). "Gene Ontology annotation based on Enzyme Commission mapping." Genomics 74;121-128.

GOA01a: GOA, DDB, FB, MGI, ZFIN (2001). "Gene Ontology annotation through association of InterPro records with GO terms."

GOA06: GOA, SIB (2006). "Electronic Gene Ontology annotations created by transferring manual GO annotations between orthologous microbial proteins."

Joyce06: Joyce AR, Reed JL, White A, Edwards R, Osterman A, Baba T, Mori H, Lesely SA, Palsson BO, Agarwalla S (2006). "Experimental and computational assessment of conditionally essential genes in Escherichia coli." J Bacteriol 188(23);8259-71. PMID: 17012394

Natter77: Natter W, Sens D, James E (1977). "Metabolism of arginine-specific messenger ribonucleic acid in Escherichia coli K-12." J Bacteriol 1977;131(1);214-23. PMID: 326762

Parsot88: Parsot C, Boyen A, Cohen GN, Glansdorff N (1988). "Nucleotide sequence of Escherichia coli argB and argC genes: comparison of N-acetylglutamate kinase and N-acetylglutamate-gamma-semialdehyde dehydrogenase with homologous and analogous enzymes." Gene 1988;68(2);275-83. PMID: 2851495

Patrick07: Patrick WM, Quandt EM, Swartzlander DB, Matsumura I (2007). "Multicopy suppression underpins metabolic evolvability." Mol Biol Evol 24(12);2716-22. PMID: 17884825

Sens77: Sens D, Natter W, James E (1977). "In vitro transcription of the Escherichia coli K-12 argA, argE, and argCBH operons." J Bacteriol 1977;130(2);642-55. PMID: 400784

Takahara07: Takahara K, Akashi K, Yokota A (2007). "Continuous spectrophotometric assays for three regulatory enzymes of the arginine biosynthetic pathway." Anal Biochem 368(2);138-47. PMID: 17651682

UniProt10: UniProt Consortium (2010). "UniProt version 2010-07 released on 2010-06-15 00:00:00." Database.

UniProtGOA11: UniProt-GOA (2011). "Gene Ontology annotation based on the manual assignment of UniProtKB Subcellular Location terms in UniProtKB/Swiss-Prot entries."

UniProtGOA11a: UniProt-GOA (2011). "Gene Ontology annotation based on manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

UniProtGOA12: UniProt-GOA (2012). "Gene Ontology annotation based on UniPathway vocabulary mapping."

Vogel74: Vogel HJ, Vogel RH (1974). "Enzymes of arginine biosynthesis and their repressive control." Adv Enzymol Relat Areas Mol Biol 1974;40(0);65-90. PMID: 4365537

WandingerNess86: Wandinger-Ness AU, Ness SA, Weiss RL (1986). "Simultaneous purification of three mitochondrial enzymes. Acetylglutamate kinase, acetylglutamyl-phosphate reductase and carbamoyl-phosphate synthetase from Neurospora crassa." J Biol Chem 261(11);4820-7. PMID: 2420793

Other References Related to Gene Regulation

Caldara06: Caldara M, Charlier D, Cunin R (2006). "The arginine regulon of Escherichia coli: whole-system transcriptome analysis discovers new genes and provides an integrated view of arginine regulation." Microbiology 152(Pt 11);3343-54. PMID: 17074904

Charlier92: Charlier D, Roovers M, Van Vliet F, Boyen A, Cunin R, Nakamura Y, Glansdorff N, Pierard A (1992). "Arginine regulon of Escherichia coli K-12. A study of repressor-operator interactions and of in vitro binding affinities versus in vivo repression." J Mol Biol 1992;226(2);367-86. PMID: 1640456

Cunin83: Cunin R, Eckhardt T, Piette J, Boyen A, Pierard A, Glansdorff N (1983). "Molecular basis for modulated regulation of gene expression in the arginine regulon of Escherichia coli K-12." Nucleic Acids Res 1983;11(15);5007-19. PMID: 6348703

Makarova01: Makarova KS, Mironov AA, Gelfand MS (2001). "Conservation of the binding site for the arginine repressor in all bacterial lineages." Genome Biol 2(4);RESEARCH0013. PMID: 11305941

Piette82: Piette J, Cunin R, Boyen A, Charlier D, Crabeel M, Van Vliet F, Glansdorff N, Squires C, Squires CL (1982). "The regulatory region of the divergent argECBH operon in Escherichia coli K-12." Nucleic Acids Res 10(24);8031-48. PMID: 6761650

Weerasinghe06: Weerasinghe JP, Dong T, Schertzberg MR, Kirchhof MG, Sun Y, Schellhorn HE (2006). "Stationary phase expression of the arginine biosynthetic operon argCBH in Escherichia coli." BMC Microbiol 6;14. PMID: 16504055


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of EcoCyc: Nucleic Acids Research 41:D605-12 2013
Page generated by SRI International Pathway Tools version 18.5 on Thu Dec 18, 2014, BIOCYC14A.