Summary: Putative TM nitroreductase
This is the Wikipedia entry entitled "Nitroreductase". More...
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Nitroreductase Edit Wikipedia article
Nitroreductases are a family of evolutionarily related proteins involved in the reduction of nitrogen-containing compounds, including those containing the nitro functional group. Members of this family utilise FMN as a cofactor and are often found to be homodimers.
Members of this family include oxygen-insensitive NAD(P)H nitroreductase (FMN-dependent nitroreductase) (6,7-dihydropteridine reductase) (EC 18.104.22.168) and NADH dehydrogenase (EC 22.214.171.124). A number of these proteins are described as oxidoreductases. They are primarily found in bacterial lineages though a number of eukaryotic homologs have been identified: C. elegans , D. melanogaster , , mouse and human . This protein is not found in photosynthetic eukaryotes. The sequences containing this entry in photosynthetic organisms are possible false positives.
Human proteins containing this domain
- Hecht HJ, Erdmann H, Park HJ, Sprinzl M, Schmid RD (December 1995). "Crystal structure of NADH oxidase from Thermus thermophilus". Nat. Struct. Biol. 2 (12): 1109–14. doi:10.1038/nsb1295-1109. PMID 8846223.
- de Oliveira IM, Henriques JA, Bonatto D (April 2007). "In silico identification of a new group of specific bacterial and fungal nitroreductases-like proteins". Biochem. Biophys. Res. Commun. 355 (4): 919–25. doi:10.1016/j.bbrc.2007.02.049. PMID 17331467.
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Putative TM nitroreductase Provide feedback
Compared with the more traditional NADH oxidase/flavin reductase family, this family is a duplication, consisting of two similar domains arranged as the subunits of the dimeric NADH oxidase/flavin reductase with one conserved active site.
Internal database links
|Similarity to PfamA using HHSearch:||Nitroreductase Nitroreductase|
External database links
This tab holds annotation information from the InterPro database.
No InterPro data for this Pfam family.
- the number of sequences which exhibit this architecture
a textual description of the architecture, e.g. Gla, EGF x 2, Trypsin.
This example describes an architecture with one
Gladomain, followed by two consecutive
EGFdomains, and finally a single
- the UniProt description of the protein sequence
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This superfamily is involved in the reduction of nitrogen containing compounds. Members of this family utilise FMN as a cofactor and are often found to be homodimers. Possible characteristics include Oxygen-insensitive NAD(P)H nitroreductase (FMN-dependent nitroreductase) (Dihydropteridine reductase) and NADH dehydrogenase. A number of the proteins are described as oxidoreductases. They are primarily found in bacterial lineages though a number of eukaryotic homologues have been identified: Caenorhabditis elegans, Drosophila melanogaster, mouse and human. These protein are not found in photosynthetic eukaryotes; sequences containing this entry in photosynthetic organisms are possible false positives.
The clan contains the following 2 members:Nitroreductase TM1586_NiRdase
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
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- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the NCBI sequence database using the family HMM
- alignment generated by searching the metagenomics sequence database using the family HMM
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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Curation and family details
This family is new in this Pfam release.
|Number in seed:||5|
|Number in full:||84|
|Average length of the domain:||203.90 aa|
|Average identity of full alignment:||23 %|
|Average coverage of the sequence by the domain:||84.37 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||1|
|Download:||download the raw HMM for this family|
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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 TM1586_NiRdase domain has been found. There are 1 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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