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CATH Superfamily 2.40.100.10

Cyclophilin-like

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:

"
Cyclophilin-like
".

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 7173: Urea amidolyase subunit 2

There are 10 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
Urea carboxylase. [EC: 6.3.4.6]
ATP + urea + HCO(3)(-) = ADP + phosphate + urea-1-carboxylate.
  • The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 3.5.1.54, thus bringing about the hydrolysis of urea to CO(2) and NH(3).
  • The enzyme from the prokaryotic bacterium Oleomonas sagaranensis can also use acetamide and formamide as substrates.
  • Formerly EC 3.5.1.45.
 530 A0A009FWR0 A0A009FWR0 A0A009GRH3 A0A009GRH3 A0A009HHR4 A0A009HHR4 A0A009JKQ6 A0A009JKQ6 A0A009KE83 A0A009KE83
(520 more...)
Allophanate hydrolase. [EC: 3.5.1.54]
Urea-1-carboxylate + H(2)O = 2 CO(2) + 2 NH(3).
  • Along with EC 3.5.2.15 and EC 3.5.1.84, forms part of the cyanuric- acid metabolism pathway, which degrades s-triazide herbicides, such as atrazine (2-chloro-4-(ethylamino)-6-(isopropylamino)-1,3,5- triazine), in bacteria.
  • The Saccharomyces cerevisiae enzyme (but not that from green algae) also catalyzes the reaction of EC 6.3.4.6, thus bringing about the hydrolysis of urea to CO(2) and NH(3) in the presence of ATP and bicarbonate.
  • The enzyme from Pseudomonas sp. strain ADP has a narrow substrate specificity, being unable to use the structurally analogous compounds urea, hydroxyurea or methylcarbamate as substrate.
 58 A0A085FHQ4 A0A085FHQ4 A0A0B9A933 A0A0B9A933 A0A1B4X336 A0A1B4X336 A0A1L8YNM7 A0A1L8YNM7 A0QUF3 A0QUF3
(48 more...)
Peptidylprolyl isomerase. [EC: 5.2.1.8]
Peptidylproline (omega=180) = peptidylproline (omega=0).
  • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
  • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
  • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
 26 A0A084ZPC4 A0A084ZPC4 A0A085G5K9 A0A085G5K9 A0A085GE83 A0A085GE83 A0A085H0X8 A0A085H0X8 A0A085HH65 A0A085HH65
(16 more...)
Biotin carboxylase. [EC: 6.3.4.14]
ATP + biotin-[carboxyl-carrier-protein] + HCO(3)(-) = ADP + phosphate + carboxy-biotin-[carboxyl-carrier-protein].
    		 10 A0A066PI30 A0A066PI30 A0A0L1HIL1 A0A0L1HIL1 A0A1I9Z7N2 A0A1I9Z7N2 B0VAZ4 B0VAZ4 S0AEV8 S0AEV8
    Acetyl-CoA carboxylase. [EC: 6.4.1.2]
    ATP + acetyl-CoA + HCO(3)(-) = ADP + phosphate + malonyl-CoA.
    • Also catalyzes transcarboxylation; the plant enzyme also carboxylates propanoyl-CoA and butanoyl-CoA.
    		 10 A0A0T9KX75 A0A0T9KX75 A0A1I9Z7N2 A0A1I9Z7N2 R9UNV5 R9UNV5 S4XJA6 S4XJA6 W0BQM1 W0BQM1
    Propionyl-CoA carboxylase. [EC: 6.4.1.3]
    ATP + propanoyl-CoA + HCO(3)(-) = ADP + phosphate + (S)-methylmalonyl- CoA.
    • Also carboxylates butanoyl-CoA and catalyzes transcarboxylation.
    		 6 A0A1I9Z7N2 A0A1I9Z7N2 B0XNG4 B0XNG4 Q4WRQ1 Q4WRQ1
    2-oxoglutarate carboxylase. [EC: 6.4.1.7]
    ATP + 2-oxoglutarate + HCO(3)(-) = ADP + phosphate + oxalosuccinate.
    • It was originally thought that this enzyme was a promoting factor for the carboxylation of 2-oxoglutarate by EC 1.1.1.41, but this has since been disproved.
    • The product of the reaction is unstable and is quickly converted into isocitrate by the action of EC 1.1.1.41.
    		 4 A0A0E9M4F0 A0A0E9M4F0 A0A1J5ST45 A0A1J5ST45
    Pyruvate carboxylase. [EC: 6.4.1.1]
    ATP + pyruvate + HCO(3)(-) = ADP + phosphate + oxaloacetate.
    • The animal enzyme requires acetyl-CoA.
    		 2 A0A1A7UL65 A0A1A7UL65
    Carbamoyl-phosphate synthase (glutamine-hydrolyzing). [EC: 6.3.5.5]
    2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 ADP + phosphate + L-glutamate + carbamoyl phosphate.
    • The product carbamoyl phosphate is an intermediate in the biosynthesis of arginine and the pyrimidine nucleotides.
    • The enzyme from Escherichia coli has three separate active sites, which are connected by a molecular tunnel that is almost 100 A in length.
    • The amidotransferase domain within the small subunit of the enzyme hydrolyzes glutamine to ammonia via a thioester intermediate.
    • The ammonia migrates through the interior of the protein, where it reacts with carboxyphosphate to produce the carbamate intermediate.
    • The carboxyphosphate intermediate is formed by the phosphorylation of hydrogencarbonate by ATP at a site contained within the N-terminal half of the large subunit.
    • The carbamate intermediate is transported through the interior of the protein to a second site within the C-terminal half of the large subunit, where it is phosphorylated by another ATP to yield the final product, carbamoyl phosphate.
    • Cf. EC 6.3.4.16.
    • Formerly EC 2.7.2.9.
    		 2 B0VAZ4 B0VAZ4
    Methylcrotonoyl-CoA carboxylase. [EC: 6.4.1.4]
    ATP + 3-methylcrotonoyl-CoA + HCO(3)(-) = ADP + phosphate + 3-methylglutaconyl-CoA.
      		 2 A3GG31 A3GG31
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