The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_0). At the point of the last release, this superfamily was named:

"
Aldolase class I
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 118665: Glutamate synthase, large subunit

There are 8 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Glutamate synthase (NADPH). [EC: 1.4.1.13]
2 L-glutamate + NADP(+) = L-glutamine + 2-oxoglutarate + NADPH.
  • The reaction takes place in the opposite direction.
  • The protein is composed of two subunits, alpha and beta.
  • The alpha subunit is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate (cf. EC 1.4.1.4).
  • The beta subunit transfers electrons to the cosubstrate.
  • The NH(3) is channeled through a 31 A channel in the active protein.
  • In the absence of the beta subunit, coupling between the two domains of the alpha subunit is compromised and some ammonium can be produced.
  • In the intact alpha-beta complex, ammonia production only takes place as part of the overall reaction.
  • Formerly EC 2.6.1.53.
4198 A0A009RY14 A0A009RY14 A0A010QWI1 A0A010QWI1 A0A010SQ82 A0A010SQ82 A0A011QXC5 A0A011QXC5 A0A014MBD8 A0A014MBD8
(4188 more...)
Glutamate synthase (ferredoxin). [EC: 1.4.7.1]
2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H(+).
  • The protein is composed of two domains, one hydrolyzing L-glutamine to NH(3) and L-glutamate (cf. EC 3.5.1.2), the other combining the produced NH(3) with 2-oxoglutarate to produce a second molecule of L-glutamate.
  • The NH(3) is channeled through a 24 A channel in the active protein.
  • No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein.
1756 A0A011N490 A0A011N490 A0A011NSM1 A0A011NSM1 A0A011QVL7 A0A011QVL7 A0A021X5L2 A0A021X5L2 A0A024LA63 A0A024LA63
(1746 more...)
Glutamate synthase (NADH). [EC: 1.4.1.14]
2 L-glutamate + NAD(+) = L-glutamine + 2-oxoglutarate + NADH.
    502 A0A060JCI0 A0A060JCI0 A0A062X613 A0A062X613 A0A081N4B5 A0A081N4B5 A0A084GFL0 A0A084GFL0 A0A084U836 A0A084U836
    (492 more...)
    Transferred entry: 1.4.1.13. [EC: 2.6.1.53]
      14 B7LHS5 B7LHS5 D8EN66 D8EN66 E1J7M9 E1J7M9 F4NHQ8 F4NHQ8 J7Q9Y8 J7Q9Y8
      (4 more...)
      Transferred entry: 2.7.1.191, 2.7.1.192, 2.7.1.193, 2.7.1.194, 2.7.1.195, 2.7.1.196, 2.7.1.197, 2.7.1.198, 2.7.1.199, 2.7.1.200, 2.7.1.201, 2.7.1.202, 2.7.1.203, 2.7.1.204, 2.7.1.205, 2.7.1.206, 2.7.1.207 and 2.7.1.208. [EC: 2.7.1.69]
        2 U2WTS2 U2WTS2
        Exopolyphosphatase. [EC: 3.6.1.11]
        (Polyphosphate)(n) + H(2)O = (polyphosphate)(n-1) + phosphate.
          2 E6LCI4 E6LCI4
          L-amino-acid oxidase. [EC: 1.4.3.2]
          An L-amino acid + H(2)O + O(2) = a 2-oxo acid + NH(3) + H(2)O(2).
            2 A0A084GFL0 A0A084GFL0
            Glutamine--pyruvate transaminase. [EC: 2.6.1.15]
            L-glutamine + pyruvate = 2-oxoglutaramate + L-alanine.
            • L-methionine can act as donor.
            • Glyoxylate can act as acceptor.
            2 O08339 O08339
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