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12  structures 173  species 2  interactions 186  sequences 4  architectures

Family: MAAL_N (PF05034)

Summary: Methylaspartate ammonia-lyase N-terminus

Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.

The Pfam group coordinates the annotation of Pfam families in Wikipedia, but we have not yet assigned a Wikipedia article to this family. If you think that a particular Wikipedia article provides good annotation, please let us know.

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:4.3.1.2 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


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 3 members:

Enolase_N MAAL_N MR_MLE_N

Alignments

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 using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...

View options

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.

  Seed
(4)
Full
(186)
Representative proteomes NCBI
(142)
Meta
(2)
RP15
(16)
RP35
(27)
RP55
(36)
RP75
(42)
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available

Key: ✓ available, x not generated, not available.

Format an alignment

  Seed
(4)
Full
(186)
Representative proteomes NCBI
(142)
Meta
(2)
RP15
(16)
RP35
(27)
RP55
(36)
RP75
(42)
Alignment:
Format:
Order:
Sequence:
Gaps:
Download/view:

Download options

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.

  Seed
(4)
Full
(186)
Representative proteomes NCBI
(142)
Meta
(2)
RP15
(16)
RP35
(27)
RP55
(36)
RP75
(42)
Raw Stockholm Download   Download   Download   Download   Download   Download   Download   Download  
Gzipped Download   Download   Download   Download   Download   Download   Download   Download  

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

External links

MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.

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...

Trees

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
Author: Bateman A, Moxon SJ
Number in seed: 4
Number in full: 186
Average length of the domain: 155.20 aa
Average identity of full alignment: 62 %
Average coverage of the sequence by the domain: 38.70 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 21.0 21.0
Trusted cut-off 21.4 36.9
Noise cut-off 20.0 18.3
Model length: 159
Family (HMM) version: 8
Download: download the raw HMM for this family

Species distribution

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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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Interactions

There are 2 interactions for this family. More...

MAAL_C MAAL_N

Structures

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 seqence.

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