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12  structures 279  species 0  interactions 301  sequences 3  architectures

Family: MAAL_N (PF05034)

Summary: Methylaspartate ammonia-lyase N-terminus

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This tab holds the annotation information that is stored in the Pfam database. As we move to using Wikipedia as our main source of annotation, the contents of this tab will be gradually replaced by the Wikipedia tab.

Methylaspartate ammonia-lyase N-terminus Provide feedback

Methylaspartate ammonia-lyase EC: catalyses the second step of fermentation of glutamate. It is a homodimer. This family represents the N-terminal region of Methylaspartate ammonia-lyase. This domain is structurally related to PF03952 [2]. This domain is associated with the catalytic domain PF07476.

Literature references

  1. Goda SK, Minton NP, Botting NP, Gani D; , Biochemistry 1992;31:10747-10756.: Cloning, sequencing, and expression in Escherichia coli of the Clostridium tetanomorphum gene encoding beta-methylaspartase and characterization of the recombinant protein. PUBMED:1420191 EPMC:1420191

  2. Levy CW, Buckley PA, Sedelnikova S, Kato Y, Asano Y, Rice DW, Baker PJ; , Structure (Camb) 2002;10:105-113.: Insights into enzyme evolution revealed by the structure of methylaspartate ammonia lyase. PUBMED:11796115 EPMC:11796115

  3. Asuncion M, Blankenfeldt W, Barlow JN, Gani D, Naismith JH; , J Biol Chem 2002;277:8306-8311.: The structure of 3-methylaspartase from Clostridium tetanomorphum functions via the common enolase chemical step. PUBMED:11748244 EPMC:11748244

Internal database links

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR022665

Methylaspartate ammonia-lyase EC catalyses the second step of fermentation of glutamate. It is a homodimer. This domain represents the N-terminal region of methylaspartate ammonia-lyase. This domain is structurally related to [ PUBMED:11796115 ]. This domain is associated with the catalytic domain .

Domain organisation

Below is a listing of the unique domain organisations or architectures in which this domain is found. More...

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Pfam Clan

This family is a member of clan Enolase_N (CL0227), which has the following description:

This domain is found at the N-terminus of the catalytic Tim barrel-like domain in enolase and other enzymes.

The clan contains the following 4 members:

Enolase_like_N Enolase_N MAAL_N MR_MLE_N


We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database (reference proteomes) using the family HMM. We also generate alignments using four representative proteomes (RP) sets and the UniProtKB sequence database. More...

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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.

Representative proteomes UniProt
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Representative proteomes UniProt

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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.

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You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.

HMM logo

HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...


This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.

Note: You can also download the data file for the tree.

Curation and family details

This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.

Curation View help on the curation process

Seed source: COG3799
Previous IDs: MAAL;
Type: Family
Sequence Ontology: SO:0100021
Author: Bateman A , Moxon SJ
Number in seed: 39
Number in full: 301
Average length of the domain: 156.8 aa
Average identity of full alignment: 52 %
Average coverage of the sequence by the domain: 38.19 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 27.0 27.0
Trusted cut-off 27.5 35.9
Noise cut-off 26.8 21.9
Model length: 159
Family (HMM) version: 16
Download: download the raw HMM for this family

Species distribution

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Colour assignments

Archea Archea Eukaryota Eukaryota
Bacteria Bacteria Other sequences Other sequences
Viruses Viruses Unclassified Unclassified
Viroids Viroids Unclassified sequence Unclassified sequence


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This visualisation provides a simple graphical representation of the distribution of this family across species. You can find the original interactive tree in the adjacent tab. More...

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The tree shows the occurrence of this domain across different species. More...


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For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the MAAL_N domain has been found. There are 12 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.

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AlphaFold Structure Predictions

The list of proteins below match this family and have AlphaFold predicted structures. Click on the protein accession to view the predicted structure.

Protein Predicted structure External Information
Q32IJ6 View 3D Structure Click here
Q3AEJ6 View 3D Structure Click here
Q3AEU2 View 3D Structure Click here
Q5V465 View 3D Structure Click here