twitter

Escherichia coli K-12 substr. MG1655 Enzyme: succinylglutamate desuccinylase



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

Synonyms: ydjS

Regulation Summary Diagram: ?

Regulation summary diagram for astE

Summary:
Succinylglutamate desuccinylase catalyzes the fifth and final reaction in the ammonia-producing arginine catabolic pathway, L-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, 142°)
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: ?

Gene-Reaction Schematic

Genetic Regulation Schematic: ?

Genetic regulation schematic for astE

GO Terms:

Biological Process: GO:0006525 - arginine metabolic process Inferred by computational analysis [UniProtGOA11a]
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 [UniProtGOA11a]
GO:0016788 - hydrolase activity, acting on ester bonds Inferred by computational analysis [GOA06, GOA01a]
GO:0046872 - metal ion binding Inferred by computational analysis [UniProtGOA11a]
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: L-arginine degradation II (AST pathway)


Sequence Features

Protein sequence of succinylglutamate desuccinylase with features indicated

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): ?

Gene local context diagram

Transcription Units:

Transcription-unit diagram

Transcription-unit diagram

Transcription-unit diagram

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.

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."

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 19.0 on Mon Apr 27, 2015, BIOCYC14B.