Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
twitter

MetaCyc Enzyme: glutamate-5-semialdehyde dehydrogenase

Gene: proA Accession Numbers: EG10767 (MetaCyc), b0243, ECK0244

Synonyms: pro(1), pro1, γ-glutamyl phosphate reductase, GPR

Species: Escherichia coli K-12 substr. MG1655

Component of: γ-glutamyl kinase-GP-reductase multienzyme complex

Subunit composition of glutamate-5-semialdehyde dehydrogenase = [ProA]4

Summary:
Glutamate-semialdehyde dehydrogenase catalyzes the second reaction, the reduction of γ-glutamyl phosphate to glutamate 5-semialdehyde, in proline biosynthesis I [Hayzer81], [Hayzer82], [Hayzer83]. Due to highly labile nature of γ-L-glutamyl 5-phosphate, the enzyme activity is measured in vitro in the reverse direction. Inhibition and kinetic studies deal with the overall reaction including the spontaneous production of pyrroline-5'-carboxylate.

The enzyme interacts with γ-glutamyl kinase, to form the γ-glutamyl kinase-GP-reductase multienzyme complex, a multimeric enzyme complex [Smith84]. It has been shown that the complex formation is essential for the functioning of γ-glutamyl kinase however, it is not a requirement for the activity of glutamate-5-semialdehyde dehydrogenase [Smith84].

Citations: [Baich71]

Locations: cytosol

Map Position: [260,727 -> 261,980]

Molecular Weight of Polypeptide: 44.63 kD (from nucleotide sequence)

Unification Links: ASAP:ABE-0000832 , CGSC:364 , DIP:DIP-10568N , EchoBASE:EB0760 , EcoGene:EG10767 , EcoliWiki:b0243 , Mint:MINT-1261639 , ModBase:P07004 , OU-Microarray:b0243 , PortEco:proA , PR:PRO_000023596 , Pride:P07004 , Protein Model Portal:P07004 , RefSeq:NP_414778 , RegulonDB:EG10767 , SMR:P07004 , String:511145.b0243 , Swiss-Model:P07004 , UniProt:P07004

Relationship Links: InterPro:IN-FAMILY:IPR000965 , InterPro:IN-FAMILY:IPR012134 , InterPro:IN-FAMILY:IPR015590 , InterPro:IN-FAMILY:IPR016161 , InterPro:IN-FAMILY:IPR016162 , InterPro:IN-FAMILY:IPR016163 , InterPro:IN-FAMILY:IPR020593 , Panther:IN-FAMILY:PTHR11063:SF1 , Pfam:IN-FAMILY:PF00171 , Prosite:IN-FAMILY:PS01223

Gene-Reaction Schematic: ?

GO Terms:

Biological Process: GO:0006561 - proline biosynthetic process Inferred from experiment Inferred by computational analysis [UniProtGOA11a, GOA06, GOA01a, Deutch84]
GO:0008152 - metabolic process Inferred by computational analysis [GOA01a]
GO:0008652 - cellular amino acid biosynthetic process Inferred by computational analysis [UniProtGOA11a]
GO:0055114 - oxidation-reduction process Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0055129 - L-proline biosynthetic process Inferred by computational analysis [UniProtGOA12]
Molecular Function: GO:0004350 - glutamate-5-semialdehyde dehydrogenase activity Inferred from experiment Inferred by computational analysis [GOA06, GOA01, GOA01a, Hayzer82, Hayzer81, Hayzer83]
GO:0050661 - NADP binding Inferred from experiment Inferred by computational analysis [GOA01a, Hayzer81]
GO:0016491 - oxidoreductase activity Inferred by computational analysis [UniProtGOA11a, GOA01a]
GO:0016620 - oxidoreductase activity, acting on the aldehyde or oxo group of donors, NAD or NADP as acceptor Inferred by computational analysis [GOA01a]
Cellular Component: GO:0005829 - cytosol Inferred from experiment Inferred by computational analysis [DiazMejia09, Ishihama08, LopezCampistrou05]
GO:0005737 - cytoplasm Inferred by computational analysis [UniProtGOA11, UniProtGOA11a, GOA06]

MultiFun Terms: metabolism biosynthesis of building blocks amino acids proline

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: glutamate-5-semialdehyde dehydrogenase

Synonyms: β-glutamylphosphate reductase, GSA dehydrogenase, γ-glutamyl phosphate reductase, GPR, GP-reductase, L-glutamate-γ-semialdehyde:NADP+ oxidoreductase (phosphorylating)

EC Number: 1.2.1.41

L-glutamate-5-semialdehyde + NADP+ + phosphate <=> γ-L-glutamyl 5-phosphate + NADPH + H+

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 opposite direction.

In Pathways: proline biosynthesis I

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Cofactors or Prosthetic Groups: NADPH [Hayzer83]

Inhibitors (Competitive): 3-(phosphonoacetylamido)-L-alanine [Hayzer83] , NADP+ [Hayzer83, Comment 1]

Inhibitors (Unknown Mechanism): Ba2+ [Hayzer82] , Co2+ [Hayzer82] , Ni2+ [Hayzer82] , p-chloromercuribenzoate [Hayzer82] , Cu2+ [Hayzer82]

Kinetic Parameters:

Substrate
Km (μM)
Citations
L-glutamate-5-semialdehyde
2200.0
[Baich71, BRENDA14]
NADP+
50.0
[Hayzer83]
phosphate
11000.0
[Baich71, BRENDA14]
phosphate
350.0
[Hayzer83, BRENDA14]

pH(opt): 7 [Hayzer82]


Subunit of: γ-glutamyl kinase-GP-reductase multienzyme complex

Species: Escherichia coli K-12 substr. MG1655

Subunit composition of γ-glutamyl kinase-GP-reductase multienzyme complex = [(ProB)4][(ProA)4]
         γ-glutamyl kinase = (ProB)4 (extended summary available)
         glutamate-5-semialdehyde dehydrogenase = (ProA)4 (summary available)

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International


Enzymatic reaction of: γ-glutamyl kinase-GP-reductase multienzyme complex

Synonyms: glutamyl kinase-GSA dehydrogenase multienzyme complex

L-glutamate + ATP + NADPH + H+ <=> ADP + L-glutamate-5-semialdehyde + NADP+ + phosphate

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

The reaction is irreversible in the direction shown.

Credits:
Imported from EcoCyc 16-Sep-2014 by Paley S , SRI International

Summary:
Glutamyl kinase requires GSA dehydrogenase for activity. [Smith84]


Sequence Features

Feature Class Location Citations Comment
Sequence-Conflict 358 -> 367
[Takemoto96, Deutch84, UniProt10a]
Alternate sequence: missing; UniProt: (in Ref. 1 and 2);

History:
10/20/97 Gene b0243 from Blattner lab Genbank (v. M52) entry merged into EcoCyc gene EG10767; confirmed by SwissProt match.


References

Baich71: Baich A (1971). "The biosynthesis of proline in Escherichia coli: phosphate-dependent glutamate -semialdehyde dehydrogenase (NADP), the second enzyme in the pathway." Biochim Biophys Acta 244(1);129-34. PMID: 4399189

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

Deutch84: Deutch AH, Rushlow KE, Smith CJ (1984). "Analysis of the Escherichia coli proBA locus by DNA and protein sequencing." Nucleic Acids Res 12(15);6337-55. PMID: 6089111

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

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."

Hayzer81: Hayzer DJ, Leisinger T (1981). "Proline biosynthesis in Escherichia coli. Stoichiometry and end-product identification of the reaction catalysed by glutamate semialdehyde dehydrogenase." Biochem J 197(2);269-74. PMID: 7034716

Hayzer82: Hayzer DJ, Leisinger T (1982). "Proline biosynthesis in Escherichia coli. Purification and characterisation of glutamate-semialdehyde dehydrogenase." Eur J Biochem 1982;121(3);561-5. PMID: 7035170

Hayzer83: Hayzer DJ, Leisinger T (1983). "Proline biosynthesis in Escherichia coli. Kinetic and mechanistic properties of glutamate semialdehyde dehydrogenase." Biochim Biophys Acta 742(2);391-8. PMID: 6337636

Ishihama08: Ishihama Y, Schmidt T, Rappsilber J, Mann M, Hartl FU, Kerner MJ, Frishman D (2008). "Protein abundance profiling of the Escherichia coli cytosol." BMC Genomics 9;102. PMID: 18304323

LopezCampistrou05: Lopez-Campistrous A, Semchuk P, Burke L, Palmer-Stone T, Brokx SJ, Broderick G, Bottorff D, Bolch S, Weiner JH, Ellison MJ (2005). "Localization, annotation, and comparison of the Escherichia coli K-12 proteome under two states of growth." Mol Cell Proteomics 4(8);1205-9. PMID: 15911532

Smith84: Smith CJ, Deutch AH, Rushlow KE (1984). "Purification and characteristics of a gamma-glutamyl kinase involved in Escherichia coli proline biosynthesis." J Bacteriol 1984;157(2);545-51. PMID: 6319365

Takemoto96: Takemoto K., Mori H., Murayama N., Kataoka K., Yano M., Itoh T., Yamamoto Y., Inokuchi H., Miki T., Hatada E., Fukuda R., Ichihara S., Mizuno T., Makino K., Nakata A., Yura T., Sampei G., Mizobuchi K. (1996). "Systematic sequencing of the Escherichia coli genome: analysis of the 4.0 - 6.0 min (189,987 - 281,416bp) region." Data submission to EMBL/GenBank/DDBJ databases on 1996-02.

UniProt10a: UniProt Consortium (2010). "UniProt version 2010-11 released on 2010-11-02 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."


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Dec 20, 2014, BIOCYC14B.