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123  structures 3862  species 0  interactions 4540  sequences 8  architectures

Family: Asp_decarbox (PF02261)

Summary: Aspartate decarboxylase

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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.

Aspartate decarboxylase Provide feedback

Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalysed by the enzyme aspartate decarboxylase EC: which requires a pyruvoyl group for its activity. It is synthesised initially as a proenzyme which is then proteolytically cleaved to an alpha (C-terminal) and beta (N-terminal) subunit and a pyruvoyl group. This family contains both chains of aspartate decarboxylase.

Literature references

  1. Albert A, Dhanaraj V, Genschel U, Khan G, Ramjee MK, Pulido R, Sibanda BL, von Delft F, Witty M, Blundell TL, Smith AG, Abell C; , Nat Struct Biol 1998;5:289-293.: Crystal structure of aspartate decarboxylase at 2.2 A resolution provides evidence for an ester in protein self-processing. PUBMED:9546220 EPMC:9546220

External database links

This tab holds annotation information from the InterPro database.

InterPro entry IPR003190

Decarboxylation of aspartate is the major route of beta-alanine production in bacteria, and is catalysed by the enzyme L-aspartate decarboxylase (ADC, EC: Beta-alanine is required for the biosynthesis of pantothenate, in which the enzyme plays a critical regulatory role. The enzyme is translated as an inactive proenzyme [ PUBMED:9169598 ], and is cleaved via self-processing at Gly23-Ser24 to yield an alpha chain (C-terminal fragment) and beta chain (N-terminal fragment). This model spans the precursor (or both beta and alpha chains) of aspartate decarboxylase. A pyruvoyl cofactor, which is covalently bound to the enzyme, is required for activity. The active site of the tetrameric enzyme is located at the interface of two subunits, with a lysine and a histidine from the beta chain of one subunit forming the active site with residues from the alpha chain of the adjacent subunit [ PUBMED:17001646 , PUBMED:15184017 , PUBMED:14633979 , PUBMED:9546220 , PUBMED:10368289 , PUBMED:3003510 ].

Gene Ontology

The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.

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 AcetylDC-like (CL0332), which has the following description:

These families are double psi-beta barrel structures.

The clan contains the following 4 members:

Asp_decarbox CDC48_N Molydop_binding PEX-2N


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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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: Pfam-B_3879 (release 5.2)
Previous IDs: none
Type: Domain
Sequence Ontology: SO:0000417
Author: Mian N , Bateman A
Number in seed: 332
Number in full: 4540
Average length of the domain: 114.20 aa
Average identity of full alignment: 53 %
Average coverage of the sequence by the domain: 88.11 %

HMM information View help on HMM parameters

HMM build commands:
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
Model details:
Parameter Sequence Domain
Gathering cut-off 25.0 25.0
Trusted cut-off 25.7 25.7
Noise cut-off 24.3 23.9
Model length: 115
Family (HMM) version: 18
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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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 Asp_decarbox domain has been found. There are 123 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
P0A790 View 3D Structure Click here
P9WIL3 View 3D Structure Click here
Q2FV23 View 3D Structure Click here