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CATH Superfamily 3.40.640.10

Type I PLP-dependent aspartate aminotransferase-like (Major domain)

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:

"
Type I PLP-dependent aspartate aminotransferase-like (Major domain)
".

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 63453: Aminotransferase, class V/Cysteine desulfurase

There are 4 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
Isopenicillin-N epimerase. [EC: 5.1.1.17]
Isopenicillin N = penicillin N.
  • Epimerization at C-5 of the 5-amino-5-carboxypentanoyl group to form penicillin N is required to make a substrate for EC 1.14.20.1, to produce cephalosporins.
  • Forms part of the penicillin biosynthesis pathway.
 47 A0A073CG66 A0A075HN87 A0A0B7DA06 A0A0D0R9U5 A0A0E1ASW0 A0A0F6UDK5 A0A0H2ZA71 A0A0P1DBM2 A0A0Q8Z6G9 A0A0R3BXP1
(37 more...)
Selenocysteine lyase. [EC: 4.4.1.16]
L-selenocysteine + reduced acceptor = selenide + L-alanine + acceptor.
  • Dithiothreitol or 2-mercaptoethanol can act as the reducing agent in the reaction.
  • The enzyme from animals does not act on cysteine, serine or chloroalanine, while the enzyme from bacteria shows activity with cysteine (cf. EC 2.8.1.7).
 5 A0A0B2Q337 A0A0B2SGA5 A0A151SS74 A0A151TX73 A0A151UIS8
Cysteine desulfurase. [EC: 2.8.1.7]
L-cysteine + acceptor = L-alanine + S-sulfanyl-acceptor.
  • The sulfur from free L-cysteine is first transferred to a cysteine residue in the active site, and then passed on to various other acceptors.
  • The enzyme is involved in the biosynthesis of iron-sulfur clusters, thio-nucleosides in tRNA, thiamine, biotin, lipoate and pyranopterin (molybdopterin).
  • In Azotobacter vinelandii, this sulfur provides the inorganic sulfide required for nitrogenous metallocluster formation.
 5 A0A024KD07 A0A0K0U322 A0A0P4UIU6 A0A1E1V883 A0A1E1VBF8
L-cysteine desulfidase. [EC: 4.4.1.28]
L-cysteine + H(2)O = sulfide + NH(3) + pyruvate.
  • The enzyme from the archaeon Methanocaldococcus jannaschii contains a [4Fe-4S] cluster and is specific for L-cysteine (cf. EC 4.4.1.1).
  • It cleaves a carbon-sulfur bond releasing sulfide and the unstable enamine product 2-aminoprop-2-enoate that tautomerizes to an imine form, which undergoes a hydrolytic deamination to form pyruvate and ammonia.
  • The same reaction can also be catalyzed by some pyridoxal-phosphate proteins (cf. EC 4.4.1.1).
 3 A0A178VKW4 Q9LGZ2 Q9M1R1
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