IntEnz

EC 1.4.7.1 - Glutamate synthase (ferredoxin)

IntEnz Enzyme Nomenclature
EC 1.4.7.1

Names

Reaction

• 12128 [IUBMB]
  2

  L-glutamate

  L-glutamate

  Name origin: UniProt - CHECKED (C)

  CHEBI:29985

  Formula: C5H8NO4
  Charge: -1

  ChEBI compound status: CHECKED (C)

  

  +

  2

  oxidized [2Fe-2S]-[ferredoxin]

  oxidized [2Fe-2S]-[ferredoxin]

  GENERIC:10000

  Is ROOT: no
  ROOT compound: GENERIC:9997

  Number of residues: 1

  [2Fe-2S]2+ [2Fe-2S](2+) Name origin: UniProt - CHECKED (C) CHEBI:33737 Formula: Fe2S2 Charge: 2 Position: undefined ChEBI compound status: CHECKED (C)

  =

  2-oxoglutarate

  2-oxoglutarate

  Name origin: UniProt - CHECKED (C)

  CHEBI:16810

  Formula: C5H4O5
  Charge: -2

  ChEBI compound status: CHECKED (C)

  

  +

  2

  H⁺

  H(+)

  Name origin: UniProt - CHECKED (C)

  CHEBI:15378

  Formula: H
  Charge: 1

  ChEBI compound status: CHECKED (C)

  

  +

  L-glutamine

  L-glutamine

  Name origin: UniProt - CHECKED (C)

  CHEBI:58359

  Formula: C5H10N2O3
  Charge: 0

  ChEBI compound status: CHECKED (C)

  

  +

  2

  reduced [2Fe-2S]-[ferredoxin]

  reduced [2Fe-2S]-[ferredoxin]

  GENERIC:10001

  Is ROOT: no
  ROOT compound: GENERIC:9997

  Number of residues: 1

  [2Fe-2S]1+ [2Fe-2S](1+) Name origin: UniProt - CHECKED (C) CHEBI:33738 Formula: Fe2S2 Charge: 1 Position: undefined ChEBI compound status: CHECKED (C)

Cofactors

• FAD
• iron-sulfur
• FMN

Comments:

Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH₃ and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH₃ with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH₃ is channeled through a 24 Å channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].

Links to other databases

References

1. Galván, F., Márquez, A.J. and Vega, J.M.
   Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardtii.
   Planta 162: 180-187 (1984).
2. Lea, P.J. and Miflin, B.J.
   Alternative route for nitrogen assimilation in higher plants.
   Nature 251: 614-616 (1974). [PMID: 4423889]
3. Ravasio, S., Dossena, L., Martin-Figueroa, E., Florencio, F. J., Mattevi, A., Morandi, P., Curti, B., Vanoni, M. A.
   Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit.
   Biochemistry 41: 8120-8133 (2002). [PMID: 12069605]
4. Navarro, F., Martin-Figueroa, E., Candau, P., Florencio, F. J.
   Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the Cyanobacterium synechocystis sp. PCC 6803: expression and assembly in Escherichia coli.
   Arch. Biochem. Biophys. 379: 267-276 (2000). [PMID: 10898944]
5. van den Heuvel, R. H., Ferrari, D., Bossi, R. T., Ravasio, S., Curti, B., Vanoni, M. A., Florencio, F. J., Mattevi, A.
   Structural studies on the synchronization of catalytic centers in glutamate synthase.
   J. Biol. Chem. 277: 24579-24583 (2002). [PMID: 11967268]
6. van den Heuvel, R. H., Svergun, D. I., Petoukhov, M. V., Coda, A., Curti, B., Ravasio, S., Vanoni, M. A., Mattevi, A.
   The active conformation of glutamate synthase and its binding to ferredoxin.
   J. Mol. Biol. 330: 113-128 (2003). [PMID: 12818206]

[EC 1.4.7.1 created 1976, modified 2012]