Summary: Quinolinate synthetase A protein
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Quinolinate synthetase A protein Provide feedback
Quinolinate synthetase catalyses the second step of the de novo biosynthetic pathway of pyridine nucleotide formation. In particular, quinolinate synthetase is involved in the condensation of dihydroxyacetone phosphate and iminoaspartate to form quinolinic acid [2]. This synthesis requires two enzymes, a FAD-containing "B protein" and an "A protein".
Literature references
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Flachmann R, Kunz N, Seifert J, Gutlich M, Wientjes FJ, Laufer A , Gassen HG; , Eur J Biochem 1988;175:221-228.: Molecular biology of pyridine nucleotide biosynthesis in Escherichia coli. Cloning and characterization of quinolinate synthesis genes nadA and nadB. PUBMED:2841129 EPMC:2841129
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Ceciliani F, Caramori T, Ronchi S, Tedeschi G, Mortarino M, Galizzi A; , Protein Expr Purif 2000;18:64-70.: Cloning, overexpression, and purification of Escherichia coli quinolinate synthetase. PUBMED:10648170 EPMC:10648170
This tab holds annotation information from the InterPro database.
InterPro entry IPR003473
Quinolinate synthetase catalyses the second step of the de novo biosynthetic pathway of pyridine nucleotide formation. In particular, quinolinate synthetase is involved in the condensation of dihydroxyacetone phosphate and iminoaspartate to form quinolinic acid [ PUBMED:10648170 ]. This synthesis requires two enzymes, an FAD-containing "B protein" and an "A protein". B protein converts L-aspartate to iminoaspartate. The A protein, NadA, converts iminoaspartate to quinolate. NadA harbours a [4Fe-4S] cluster [ PUBMED:18803397 ].
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
Molecular function | 4 iron, 4 sulfur cluster binding (GO:0051539) |
quinolinate synthetase A activity (GO:0008987) | |
Biological process | NAD biosynthetic process (GO:0009435) |
Domain organisation
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Alignments
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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.
Seed (520) |
Full (5962) |
Representative proteomes | UniProt (30729) |
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RP15 (848) |
RP35 (2933) |
RP55 (6047) |
RP75 (10505) |
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PP/heatmap | 1 |
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
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Seed (520) |
Full (5962) |
Representative proteomes | UniProt (30729) |
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RP15 (848) |
RP35 (2933) |
RP55 (6047) |
RP75 (10505) |
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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
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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: | Pfam-B_1915 (release 5.4) |
Previous IDs: | none |
Type: | Family |
Sequence Ontology: | SO:0100021 |
Author: |
Bateman A |
Number in seed: | 520 |
Number in full: | 5962 |
Average length of the domain: | 308.50 aa |
Average identity of full alignment: | 39 % |
Average coverage of the sequence by the domain: | 86.04 % |
HMM information
HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 57096847 -E 1000 --cpu 4 HMM pfamseq
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Model details: |
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Model length: | 299 | ||||||||||||
Family (HMM) version: | 18 | ||||||||||||
Download: | download the raw HMM for this family |
Species distribution
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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 NadA domain has been found. There are 30 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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