Summary: Phenazine biosynthesis protein A/B
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Phenazine biosynthesis protein A/B Provide feedback
No Pfam abstract.
Mavrodi DV, Ksenzenko VN, Bonsall RF, Cook RJ, Boronin AM, Thomashow LS; , J Bacteriol 1998;180:2541-2548.: A seven-gene locus for synthesis of phenazine-1-carboxylic acid by Pseudomonas fluorescens 2-79. PUBMED:9573209 EPMC:9573209
Internal database links
|SCOOP:||Adeno_GP19K SnoaL SnoaL_2 SnoaL_4 DUF4440|
|Similarity to PfamA using HHSearch:||SnoaL_2|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004964The phenazine biosynthesis proteins A and B are involved in the biosynthesis of this antibiotic. Phenazine is a nitrogen-containing heterocyclic molecule with important implications in virulence, competition and biological control [PUBMED:9573209].
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Biological process||antibiotic biosynthetic process (GO:0017000)|
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This superfamily contains a variety of enzymes such as Scytalone dehydratase, Delta-5-3-ketosteroid isomerase, Limonene-1,2-epoxide hydrolase among others. The family also includes presumed non-enzymatic homologues such as NTF2.
The clan contains the following 27 members:CaMKII_AD DUF1348 DUF2358 DUF3225 DUF3804 DUF3828 DUF3887 DUF4440 DUF4467 DUF4864 DUF4878 LEH Lumazine_bd_2 MBA1 MecA_N Mtr2 NTF2 PHZA_PHZB Ring_hydroxyl_B Scytalone_dh SnoaL SnoaL_2 SnoaL_3 SnoaL_4 Tim44 VirB8 WI12
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_4020 (release 6.5)|
|Number in seed:||4|
|Number in full:||836|
|Average length of the domain:||148.20 aa|
|Average identity of full alignment:||77 %|
|Average coverage of the sequence by the domain:||95.22 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 80369284 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||9|
|Download:||download the raw HMM for this family|
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
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 PHZA_PHZB domain has been found. There are 21 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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