D
IPR047921

LACTB2-like, MBL-fold metallo hydrolase domain

InterPro entry
Short nameLACTB2-like_MBL-fold
Overlapping
homologous
superfamilies
 
domain relationships

Description

Members of this subgroup belong to the MBL-fold metallo-hydrolase superfamily which is comprised mainly of hydrolytic enzymes which carry out a variety of biological functions. The class B metal beta-lactamases (MBLs) from which this fold was named are only a small fraction of the activities which are included in this superfamily. Activities carried out by superfamily members include class B beta-lactamases, hydroxyacylglutathione hydrolases, AHL (acyl homoserine lactone) lactonases, persulfide dioxygenases, flavodiiron proteins, cleavage and polyadenylation specificity factors such as the Int9 and Int11 subunits of Integrator, Sdsa1-like and AtsA-like arylsulfatases, 5'-exonucleases human SNM1A and yeast Pso2p, ribonuclease J and ribonuclease Z, cyclic nucleotide phosphodiesterases, insecticide hydrolases, and proteins required for natural transformation competence. Classical members of the superfamily are di-, or less commonly mono-, zinc-ion-dependent hydrolases, however the diversity of biological roles is reflected in variations in the active site metallo-chemistry
[6, 2, 4, 3, 5, 1]
.

This entry represents the MBL-fold hydrolase domain from metazoan and fungal proteins, including human endoribonuclease LACTB2
[8]
, the orthologue from Drosophila Beta-lactamase-like protein 2 homologue, fungal atrochrysone carboxyl ACP thioesterases
[7]
, among others.

References

1.The 3-D structure of a zinc metallo-beta-lactamase from Bacillus cereus reveals a new type of protein fold. Carfi A, Pares S, Duee E, Galleni M, Duez C, Frere JM, Dideberg O. EMBO J. 14, 4914-21, (1995). View articlePMID: 7588620

2.Extracting protein alignment models from the sequence database. Neuwald AF, Liu JS, Lipman DJ, Lawrence CE. Nucleic Acids Res. 25, 1665-77, (1997). View articlePMID: 9108146

3.Expansion of the zinc metallo-hydrolase family of the beta-lactamase fold. Daiyasu H, Osaka K, Ishino Y, Toh H. FEBS Lett. 503, 1-6, (2001). View articlePMID: 11513844

4.An evolutionary classification of the metallo-beta-lactamase fold proteins. Aravind L. In Silico Biol. (Gedrukt) 1, 69-91, (1999). PMID: 11471246

5.Metallo-beta-lactamases (classification, activity, genetic organization, structure, zinc coordination) and their superfamily. Bebrone C. Biochem. Pharmacol. 74, 1686-701, (2007). View articlePMID: 17597585

6.Disruption of NCOA2 by recurrent fusion with LACTB2 in colorectal cancer. Yu J, Wu WK, Liang Q, Zhang N, He J, Li X, Zhang X, Xu L, Chan MT, Ng SS, Sung JJ. Oncogene 35, 187-95, (2016). PMID: 25823027

7.Heterologous Biosynthesis of Tetrahydroxanthone Dimers: Determination of Key Factors for Selective or Divergent Synthesis. Wei X, Chen X, Chen L, Yan D, Wang WG, Matsuda Y. J Nat Prod 84, 1544-1549, (2021). PMID: 33891392

8.Identification of LACTB2, a metallo-β-lactamase protein, as a human mitochondrial endoribonuclease. Levy S, Allerston CK, Liveanu V, Habib MR, Gileadi O, Schuster G. Nucleic Acids Res. 44, 1813-32, (2016). View articlePMID: 26826708

Cross References

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