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discounted EARLY registration ends Dec 31, 2014
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
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Escherichia coli K-12 substr. MG1655 Enzyme: succinylglutamate desuccinylase



Gene: astE Accession Numbers: G6940 (EcoCyc), b1744, ECK1742

Synonyms: ydjS

Regulation Summary Diagram: ?

Summary:
Succinylglutamate desuccinylase catalyzes the fifth and final reaction in the ammonia-producing arginine catabolic pathway, arginine degradation II (AST pathway). The activity has only been assayed in crude cell extracts, and thus there is little direct evidence for the function of the astE gene product [Schneider98].

Deletion of astE enhances tolerance to n-butanol [Reyes11].

Expression of the enzymes of the AST pathway is regulated by arginine and nitrogen availability [Schneider98] via ArgR and NtrC [Kiupakis02].

Locations: cytosol

Map Position: [1,823,979 <- 1,824,947] (39.31 centisomes)
Length: 969 bp / 322 aa

Molecular Weight of Polypeptide: 35.8 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0005815 , EchoBASE:EB3751 , EcoGene:EG13995 , EcoliWiki:b1744 , ModBase:P76215 , OU-Microarray:b1744 , PortEco:astE , PR:PRO_000022179 , Protein Model Portal:P76215 , RefSeq:NP_416258 , RegulonDB:G6940 , SMR:P76215 , String:511145.b1744 , UniProt:P76215

Relationship Links: InterPro:IN-FAMILY:IPR007036 , InterPro:IN-FAMILY:IPR016681 , PDB:Structure:1YW6 , Pfam:IN-FAMILY:PF04952

Gene-Reaction Schematic: ?

Genetic Regulation Schematic: ?

GO Terms:

Biological Process: GO:0006525 - arginine metabolic process Inferred by computational analysis [UniProtGOA11]
GO:0006950 - response to stress Inferred by computational analysis [UniProtGOA11]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0019544 - arginine catabolic process to glutamate Inferred by computational analysis [GOA06, GOA01a]
GO:0019545 - arginine catabolic process to succinate Author statement Inferred by computational analysis [UniProtGOA12, GOA01a, Schneider98]
Molecular Function: GO:0005515 - protein binding Inferred from experiment [Rajagopala14]
GO:0009017 - succinylglutamate desuccinylase activity Inferred from experiment Inferred by computational analysis [GOA01, GOA01a, Schneider98]
GO:0008270 - zinc ion binding Inferred by computational analysis [GOA06, GOA01a]
GO:0016787 - hydrolase activity Inferred by computational analysis [UniProtGOA11]
GO:0016788 - hydrolase activity, acting on ester bonds Inferred by computational analysis [GOA06, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11]
Cellular Component: GO:0005829 - cytosol Inferred by computational analysis [DiazMejia09]

MultiFun Terms: metabolism carbon utilization amino acids

Essentiality data for astE 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 1% glycerol Yes 37 Aerobic 7.2 0.35 Yes [Joyce06, Comment 2]
MOPS medium with 0.4% glucose Yes 37 Aerobic 7.2 0.22 Yes [Baba06, Comment 1]
Yes [Feist07, Comment 3]

Credits:
Last-Curated ? 14-Oct-2011 by Keseler I , SRI International


Enzymatic reaction of: succinylglutamate desuccinylase

EC Number: 3.5.1.96

N2-succinylglutamate + H2O <=> succinate + L-glutamate

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

The reaction is favored in the direction shown.

In Pathways: arginine degradation II (AST pathway)


Sequence Features

Feature Class Location Citations Comment
Metal-Binding-Site 53
[UniProt10a]
UniProt: Zinc; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 56
[UniProt10a]
UniProt: Zinc; Non-Experimental Qualifier: by similarity;
Metal-Binding-Site 147
[UniProt10a]
UniProt: Zinc; Non-Experimental Qualifier: by similarity;
Active-Site 210
[UniProt10a]
UniProt: Non-Experimental Qualifier: potential;


Gene Local Context (not to scale): ?

Transcription Units:

Notes:

History:
Markus Krummenacker on Tue Oct 14, 1997:
Gene object created from Blattner lab Genbank (v. M52) entry.


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

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

Kiupakis02: Kiupakis AK, Reitzer L (2002). "ArgR-independent induction and ArgR-dependent superinduction of the astCADBE operon in Escherichia coli." J Bacteriol 184(11);2940-50. PMID: 12003934

Rajagopala14: Rajagopala SV, Sikorski P, Kumar A, Mosca R, Vlasblom J, Arnold R, Franca-Koh J, Pakala SB, Phanse S, Ceol A, Hauser R, Siszler G, Wuchty S, Emili A, Babu M, Aloy P, Pieper R, Uetz P (2014). "The binary protein-protein interaction landscape of Escherichia coli." Nat Biotechnol 32(3);285-90. PMID: 24561554

Reyes11: Reyes LH, Almario MP, Kao KC (2011). "Genomic library screens for genes involved in n-butanol tolerance in Escherichia coli." PLoS One 6(3);e17678. PMID: 21408113

Schneider98: Schneider BL, Kiupakis AK, Reitzer LJ (1998). "Arginine catabolism and the arginine succinyltransferase pathway in Escherichia coli." J Bacteriol 1998;180(16);4278-86. PMID: 9696779

UniProt10a: 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 manual assignment of UniProtKB keywords in UniProtKB/Swiss-Prot entries."

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

Other References Related to Gene Regulation

Fraley98: Fraley CD, Kim JH, McCann MP, Matin A (1998). "The Escherichia coli starvation gene cstC is involved in amino acid catabolism." J Bacteriol 1998;180(16);4287-90. PMID: 9696780


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 Fri Dec 19, 2014, BIOCYC13B.