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CATH Superfamily 3.90.230.10

Creatinase/methionine aminopeptidase superfamily

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:

"
Creatinase/methionine aminopeptidase superfamily
".

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 9058: Probable Xaa-Pro aminopeptidase P

There are 7 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
Xaa-Pro aminopeptidase. [EC: 3.4.11.9]
Release of any N-terminal amino acid, including proline, that is linked to proline, even from a dipeptide or tripeptide.
  • Generally membrane bound enzyme present in both mammalian and bacterial cells.
  • Belongs to peptidase family M24B.
 429 A0A017HBS9 A0A017HRP8 A0A021WXH1 A0A023BBB1 A0A024KFM7 A0A024LRK1 A0A060I393 A0A060QDR3 A0A060QLI7 A0A060R9E8
(419 more...)
Xaa-Pro dipeptidase. [EC: 3.4.13.9]
Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.
  • Possibly thiol dependent.
  • Cytosolic from most animal tissues.
  • Belongs to peptidase family M24A.
  • Formerly EC 3.4.3.7.
 101 A0A060S035 A0A067AKX6 A0A069RDQ8 A0A0D1CTB4 A0A0E9EIS4 A0A0F5MPQ7 A0A0F7KRK9 A0A0H3AKS0 A0A0H3QE83 A0A0H5B8I2
(91 more...)
Adenosylhomocysteinase. [EC: 3.3.1.1]
S-adenosyl-L-homocysteine + H(2)O = L-homocysteine + adenosine.
  • The NAD(+) cofactor appears to bring about a transient oxidation at C-3' of the 5'-deoxyadenosine residue, thus labilizing the thioether bond cf. EC 5.5.1.4.
 1 R9P3J3
Ribonuclease P. [EC: 3.1.26.5]
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
  • Essential for tRNA processing; generates 5'-termini of mature tRNA molecules.
 1 G6XLB4
Acyl-[acyl-carrier-protein]--UDP-N-acetylglucosamine O-acyltransferase. [EC: 2.3.1.129]
(R)-3-hydroxytetradecanoyl-[acyl-carrier-protein] + UDP-N-acetyl-alpha-D- glucosamine = [acyl-carrier-protein] + UDP-3-O-(3-hydroxytetradecanoyl)- N-acetyl-alpha-D-glucosamine.
  • Involved with EC 2.4.1.182 and EC 2.7.1.130 in the biosynthesis of the phosphorylated glycolipid, lipid A, in the outer membrane of Escherichia coli.
 1 Q92HP6
Deleted entry. [EC: 1.3.99.1]
    		1 U2WW09
    Dipeptidyl-peptidase IV. [EC: 3.4.14.5]
    Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, from a polypeptide, preferentially when Yaa is Pro, provided Zaa is neither Pro nor hydroxyproline.
    • A membrane-bound serine-type peptidase in mammals.
    • EC 3.4.14.11 catalyzes a similar reaction.
    • Belongs to peptidase family S9B.
    		 1 A0A060S035