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CATH Superfamily 3.90.190.20

Mur ligase, C-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Mur ligase, C-terminal 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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 14 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
UDP-N-acetylmuramate--L-alanine ligase. [EC: 6.3.2.8]
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanine = ADP + phosphate + UDP- N-acetyl-alpha-D-muramoyl-L-alanine.
  • Involved in the synthesis of a cell-wall peptide.
 1490 A0A009HC65 A0A009HTJ2 A0A009KIK7 A0A009PHI7 A0A009RHZ7 A0A023PD81 A0A023YS69 A0A025CLC5 A0A026V7I8 A0A029IF13
(1480 more...)
UDP-N-acetylmuramoyl-L-alanine--D-glutamate ligase. [EC: 6.3.2.9]
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + D-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate.
  • Involved in the synthesis of a cell-wall peptide in bacteria.
 992 A0A023PBD6 A0A028AH27 A0A028DP02 A0A029IDW8 A0A029J2N9 A0A031WCS1 A0A037YQ92 A0A049E9Q3 A0A062MX61 A0A062X778
(982 more...)
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--2,6-diaminopimelate ligase. [EC: 6.3.2.13]
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + meso-2,6- diaminoheptanedioate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L- alanyl-D-gamma-glutamyl-meso-2,6-diaminoheptanedioate.
  • Involved in the synthesis of a cell-wall peptide.
  • This enzyme adds diaminopimelate in Gram-negative organisms and in some Gram-positive organisms; in others EC 6.3.2.7 adds lysine instead.
  • It is the amino group of the L-center of the diaminopimelate that is acylated.
 306 A0A017NJ80 A0A049ECC3 A0A069ZXI4 A0A078RH08 A0A083ZCD0 A0A0A8F6R4 A0A0B6V6E1 A0A0C5X8P6 A0A0D6HHZ6 A0A0E0UF70
(296 more...)
Tetrahydrofolate synthase. [EC: 6.3.2.17]
ATP + tetrahydropteroyl-(gamma-Glu)(n) + L-glutamate = ADP + phosphate + tetrahydropteroyl-(gamma-Glu)(n+1).
  • In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.12, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates (H(4)folate).
  • In contrast, the activities are located on separate proteins in most eukaryotes studied to date.
  • In Arabidopsis thaliana, this enzyme is present as distinct isoforms in the mitochondria, the cytosol and the chloroplast.
  • Each isoform is encoded by a separate gene, a situation that is unique among eukaryotes.
  • As the affinity of folate-dependent enzymes increases markedly with the number of glutamic residues, the tetrahydropteroyl polyglutamates are the preferred coenzymes of C(1) metabolism.
  • The enzymes from different sources (particularly eukaryotes versus prokaryotes) have different substrate specificities with regard to one-carbon substituents and the number of glutamate residues present on the tetrahydrofolates.
 73 A0A045GZ48 A0A069XRP0 A0A070T4Q8 A0A070UX06 A0A0A0FDP3 A0A0B0DW93 A0A0E0U0W8 A0A0E1LZT2 A0A0E1T624 A0A0H3LIL9
(63 more...)
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--L-lysine ligase. [EC: 6.3.2.7]
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + L-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D- glutamyl-L-lysine.
  • Involved in the synthesis of a cell-wall peptide.
  • This enzyme adds lysine in some Gram-positive organisms; in others and in Gram-negative organisms EC 6.3.2.13 adds 2,6-diaminopimelate instead.
 70 A0A0E1AIW6 A0A0E1EIP4 A0A0E1EPU1 A0A0E1VKS0 A0A0E1X6V3 A0A0E7MX78 A0A0E8ZC32 A0A0H3K7Y4 A0A0H3MVS2 A0A0U1B2S3
(60 more...)
Dihydrofolate synthase. [EC: 6.3.2.12]
ATP + 7,8-dihydropteroate + L-glutamate = ADP + phosphate + 7,8- dihydropteroylglutamate.
  • In some bacteria, a single protein catalyzes both this activity and that of EC 6.3.2.17, the combined activity of which leads to the formation of the coenzyme polyglutamated tetrahydropteroate (H(4)PteGlu(n)), i.e. various tetrahydrofolates.
  • In contrast, the activities are located on separate proteins in most eukaryotes studied to date.
  • This enzyme is reponsible for attaching the first glutamate residue to dihydropteroate to form dihydrofolate and is present only in those organisms that have the ability to synthesize tetrahydrofolate de novo, e.g. plants, most bacteria, fungi and protozoa.
 51 A0A045GZ48 A0A069XRP0 A0A070T4Q8 A0A070UX06 A0A0A0FDP3 A0A0E0U0W8 A0A0E1LZT2 A0A0E1T624 A0A0H3LIL9 A0A0H3M8P3
(41 more...)
UDP-N-acetylmuramoyl-tripeptide--D-alanyl-D-alanine ligase. [EC: 6.3.2.10]
ATP + UDP-N-acetylmuramoyl-L-alanyl-gamma-D-glutamyl-L-lysine + D-alanyl- D-alanine = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl-gamma-D- glutamyl-L-lysyl-D-alanyl-D-alanine.
  • Involved with EC 6.3.2.4, EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8 and EC 6.3.2.9 in the synthesis of a cell-wall peptide.
  • Also catalyzes the reaction when the C-terminal residue of the tripeptide is meso-2,4-diaminoheptanedioate (acylated at its L-center), linking the D-Ala--D-Ala to the carboxy group of the L-center.
  • Formerly EC 6.3.2.15.
 45 A0A024L7R2 A0A069XVA9 A0A081XYR6 A0A0A7X2H9 A0A0E1LT70 A0A0E8NQ63 A0A0H3BJ28 A0A0H3LB03 A0A0H3M6I8 A0A0H3MQ51
(35 more...)
UDP-N-acetylmuramoyl-L-alanine--L-glutamate ligase. [EC: 6.3.2.53]
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanine + L-glutamate = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-L-glutamate.
  • The enzyme, characterized from the bacterium Xanthomonas oryzae, catalyzes the ligation of a terminal L-glutamate to UDP-N-acetyl- alpha-D-muramoyl-L-alanine.
  • The combined activity of this enzyme and EC 5.1.1.23 provides an alternative route for incorporating D-glutamate into peptidoglycan, replacing the more common combination of EC 5.1.1.3 and EC 6.3.2.9.
 21 A0A0G9AV24 A0A0K0GNE4 A0A0U4VUF5 A0A0U5FG42 A0A1S0V5L0 A0A1T1S8Z3 A0A3G2W3Y5 A0A432KRF2 A4X981 B0RQN8
(11 more...)
Cyanophycin synthase (L-aspartate-adding). [EC: 6.3.2.29]
ATP + (L-Asp(4-L-Arg))(n) + L-Asp = ADP + phosphate + (L-Asp(4-L- Arg))(n)-L-Asp.
  • Both this enzyme and EC 6.3.2.30 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store.
  • Both enzymes are found in the same protein but have different active sites.
  • Both L-Asp and L-Arg must be present before either enzyme will display significant activity.
 7 A0A1W5CCM8 A0A1Z4KKL9 O86109 P56947 P58572 P73833 Q9KGY4
Cyanophycin synthase (L-arginine-adding). [EC: 6.3.2.30]
ATP + (L-Asp(4-L-Arg))(n)-L-Asp + L-Arg = ADP + phosphate + (L-Asp(4-L- Arg))(n+1).
  • Both this enzyme and EC 6.3.2.29 are required for the elongation of cyanophycin, which is a protein-like cell inclusion that is unique to cyanobacteria and acts as a temporary nitrogen store.
  • Both enzymes are found in the same protein but have different active sites.
  • Both L-Asp and L-Arg must be present before either enzyme will display significant activity.
  • Canavanine and lysine can be incoporated into the polymer instead of arginine.
 7 A0A1W5CCM8 A0A1Z4KKL9 O86109 P56947 P58572 P73833 Q9KGY4
D-alanine--D-alanine ligase. [EC: 6.3.2.4]
ATP + 2 D-alanine = ADP + phosphate + D-alanyl-D-alanine.
  • Involved with EC 6.3.2.7 or EC 6.3.2.13, EC 6.3.2.8, EC 6.3.2.9 and EC 6.3.2.10 in the synthesis of a cell-wall peptide.
 6 A0A097KIQ0 A0A0F7XK32 O84767 Q821S4 Q9PLG1 Q9Z701
Dihydropteroate synthase. [EC: 2.5.1.15]
6-hydroxymethyl-7,8-dihydropterin diphosphate + 4-aminobenzoate = diphosphate + dihydropteroate.
  • The enzyme participates in the biosynthetic pathways for folate (in bacteria, plants and fungi) and methanopterin (in archaea).
  • The enzyme exists in varying types of multifunctional proteins in different organisms.
  • The enzyme from the plant Arabidopsis thaliana also harbors the activity of EC 2.7.6.3, while the enzyme from yeast Saccharomyces cerevisiae is trifunctional with the two above mentioned activities as well as EC 4.1.2.25.
 3 B0R3B1 D4GW05 Q9HS44
UDP-N-acetylmuramate L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioate ligase. [EC: 6.3.2.45]
ATP + UDP-N-acetyl-alpha-D-muramate + L-alanyl-gamma-D-glutamyl-meso-2,6- diaminoheptanedioate = ADP + phosphate + UDP-N-acetylmuramoyl-L-alanyl- gamma-D-glutamyl-meso-2,6-diaminoheptanedioate.
  • The enzyme catalyzes the reincorporation into peptidoglycan of the tripeptide L-alanyl-gamma-D-glutamyl-2,6-meso-diaminoheptanedioate released during the maturation and constant remodeling of this bacterial cell wall polymer that occur during cell growth and division.
  • The enzyme can also use the tetrapeptide L-alanyl-gamma-D-glutamyl- meso-2,6-diaminoheptanedioyl-D-alanine or the pentapeptide L-alanyl- gamma-D-glutamyl-meso-2,6-diaminoheptanedioyl-D-alanyl-D-alanine in vivo and in vitro.
 3 A0A2S5ZSL6 P37773 P43948
UDP-N-acetylmuramoyl-L-alanyl-D-glutamate--D-lysine ligase. [EC: 6.3.2.37]
ATP + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-D-glutamate + D-lysine = ADP + phosphate + UDP-N-acetyl-alpha-D-muramoyl-L-alanyl-gamma-D- glutamyl-N(epsilon)-D-lysine.
  • Involved in the synthesis of cell-wall peptidoglycan.
  • The D-lysine is attached to the peptide chain at the N(6) position.
  • The enzyme from Thermotoga maritima also performs the reaction of EC 6.3.2.7.
  • Formerly EC 6.3.2.n1.
 2 G4FHF1 Q9WY79