Summary: Orn/Lys/Arg decarboxylase, major domain
Pfam includes annotations and additional family information from a range of different sources. These sources can be accessed via the tabs below.
This is the Wikipedia entry entitled "Group III pyridoxal-dependent decarboxylases". More...
Group III pyridoxal-dependent decarboxylases Edit Wikipedia article
Orn/Lys/Arg decarboxylase, N-terminal domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() crystallographic structure of a plp-dependent ornithine decarboxylase from lactobacillus 30a to 3.1 angstroms resolution | |||||||||
Identifiers | |||||||||
Symbol | OKR_DC_1_N | ||||||||
Pfam | PF03709 | ||||||||
Pfam clan | CL0304 | ||||||||
InterPro | IPR005308 | ||||||||
PROSITE | PDOC00585 | ||||||||
SCOP2 | 1ord / SCOPe / SUPFAM | ||||||||
|
Orn/Lys/Arg decarboxylase, major domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() crystallographic structure of a plp-dependent ornithine decarboxylase from lactobacillus 30a to 3.1 angstroms resolution | |||||||||
Identifiers | |||||||||
Symbol | OKR_DC_1 | ||||||||
Pfam | PF01276 | ||||||||
Pfam clan | CL0061 | ||||||||
InterPro | IPR000310 | ||||||||
PROSITE | PDOC00585 | ||||||||
SCOP2 | 1ord / SCOPe / SUPFAM | ||||||||
|
Orn/Lys/Arg decarboxylase, C-terminal domain | |||||||||
---|---|---|---|---|---|---|---|---|---|
![]() crystallographic structure of a plp-dependent ornithine decarboxylase from lactobacillus 30a to 3.1 angstroms resolution | |||||||||
Identifiers | |||||||||
Symbol | OKR_DC_1_C | ||||||||
Pfam | PF03711 | ||||||||
InterPro | IPR008286 | ||||||||
PROSITE | PDOC00585 | ||||||||
SCOP2 | 1ord / SCOPe / SUPFAM | ||||||||
|
In molecular biology, group III pyridoxal-dependent decarboxylases are a family of bacterial enzymes comprising ornithine decarboxylase EC 4.1.1.17, lysine decarboxylase EC 4.1.1.18 and arginine decarboxylase EC 4.1.1.19.[1]
Structure
These enzymes consist of several conserved domains. The N-terminal domain has a flavodoxin-like fold, and is termed the "wing" domain because of its position in the overall 3D structure. Ornithine decarboxylase from Lactobacillus 30a (L30a OrnDC) is representative of the large, pyridoxal-5'-phosphate-dependent decarboxylases that act on lysine, arginine or ornithine. The crystal structure of the L30a OrnDC has been solved to 3.0 A resolution. Six dimers related by C6 symmetry compose the enzymatically active dodecamer (approximately 106 Da). Each monomer of L30a OrnDC can be described in terms of five sequential folding domains. The amino-terminal domain, residues 1 to 107, consists of a five-stranded beta-sheet termed the "wing" domain. Two wing domains of each dimer project inward towards the centre of the dodecamer and contribute to dodecamer stabilisation.[2] The major domain contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group.[2]
References
- ^ Sandmeier E, Hale TI, Christen P (1994). "Multiple evolutionary origin of pyridoxal-5'-phosphate-dependent amino acid decarboxylases". Eur. J. Biochem. 221 (3): 997–1002. PMID 8181483.
{{cite journal}}
: Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link) - ^ a b Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML (1995). "Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution". J. Mol. Biol. 252 (5): 643–55. doi:10.1006/jmbi.1995.0526. PMID 7563080.
{{cite journal}}
: Unknown parameter|month=
ignored (help)CS1 maint: multiple names: authors list (link) Cite error: The named reference "pmid7563080" was defined multiple times with different content (see the help page).
This page is based on a Wikipedia article. The text is available under the Creative Commons Attribution/Share-Alike License.
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.
Orn/Lys/Arg decarboxylase, major domain Provide feedback
No Pfam abstract.
Literature references
-
Momany C, Ernst S, Ghosh R, Chang NL, Hackert ML; , J Mol Biol 1995;252:643-655.: Crystallographic structure of a PLP-dependent ornithine decarboxylase from Lactobacillus 30a to 3.0 A resolution. PUBMED:7563080 EPMC:7563080
Internal database links
SCOOP: | Aminotran_1_2 Aminotran_5 Beta_elim_lyase Cys_Met_Meta_PP DegT_DnrJ_EryC1 GDC-P Pyridoxal_deC SepSecS SHMT |
Similarity to PfamA using HHSearch: | Aminotran_1_2 Aminotran_5 Pyridoxal_deC DegT_DnrJ_EryC1 Beta_elim_lyase |
External database links
PROSITE: | PDOC00585 |
SCOP: | 1ord |
This tab holds annotation information from the InterPro database.
InterPro entry IPR000310
Pyridoxal-dependent decarboxylases are bacterial proteins acting on ornithine, lysine, arginine and related substrates [ PUBMED:8181483 ]. One of the regions of sequence similarity contains a conserved lysine residue, which is the site of attachment of the pyridoxal-phosphate group. Ornithine decarboxylase is a dodecamer composed of six homodimers and catalyzes the decarboxylation of tryptophan. Arginine decarboxylase catalyzes the decarboxylation of arginine and lysine decarboxylase catalyzes the decarboxylation of lysine. Members of this family are widely found in all three forms of life [ PUBMED:8181483 , PUBMED:7663340 , PUBMED:9405048 , PUBMED:9063963 , PUBMED:8112347 , PUBMED:7748903 , PUBMED:10586514 , PUBMED:17504214 , PUBMED:17109392 , PUBMED:10223296 , PUBMED:9914259 , PUBMED:10800595 , PUBMED:11933250 , PUBMED:10673430 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | catalytic activity (GO:0003824) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
Loading domain graphics...
Pfam Clan
This family is a member of clan PLP_aminotran (CL0061), which has the following description:
This superfamily contains a variety of PLP-dependent enzymes.
The clan contains the following 16 members:
Alliinase_C Aminotran_1_2 Aminotran_3 Aminotran_5 Asp_aminotransf Beta_elim_lyase ComK Cys_Met_Meta_PP DegT_DnrJ_EryC1 GDC-P Met_gamma_lyase OKR_DC_1 Pyridoxal_deC SelA SepSecS SHMTAlignments
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...
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 (8) |
Full (5324) |
Representative proteomes | UniProt (30301) |
||||
---|---|---|---|---|---|---|---|
RP15 (646) |
RP35 (2668) |
RP55 (5436) |
RP75 (10024) |
||||
Jalview | |||||||
HTML | |||||||
PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
available,
not generated,
— not available.
Format an alignment
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 (8) |
Full (5324) |
Representative proteomes | UniProt (30301) |
||||
---|---|---|---|---|---|---|---|
RP15 (646) |
RP35 (2668) |
RP55 (5436) |
RP75 (10024) |
||||
Raw Stockholm | |||||||
Gzipped |
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...
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
Seed source: | Prosite |
Previous IDs: | none |
Type: | Domain |
Sequence Ontology: | SO:0000417 |
Author: |
Finn RD |
Number in seed: | 8 |
Number in full: | 5324 |
Average length of the domain: | 341.3 aa |
Average identity of full alignment: | 29 % |
Average coverage of the sequence by the domain: | 61.55 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 61295632 -E 1000 --cpu 4 HMM pfamseq
|
||||||||||||
Model details: |
|
||||||||||||
Model length: | 417 | ||||||||||||
Family (HMM) version: | 23 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
Sunburst controls
HideWeight segments by...
Change the size of the sunburst
Colour assignments
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
![]() |
Selections
Align selected sequences to HMM
Generate a FASTA-format file
Clear selection
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...
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
Loading...
Please note: for large trees this can take some time. While the tree is loading, you can safely switch away from this tab but if you browse away from the family page entirely, the tree will not be loaded.
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 OKR_DC_1 domain has been found. There are 117 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.
Loading structure mapping...
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.