Summary: TENA/THI-4/PQQC family
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TENA/THI-4/PQQC family Provide feedback
Members of this family are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TENA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase . The THI-4 protein, which is involved in thiamine biosynthesis, is also a member of this family. The C-terminal part of these proteins consistently show significant sequence similarity to TENA proteins. This similarity was first noted with the Neurospora crassa THI-4 . This family includes bacterial coenzyme PQQ synthesis protein C or PQQC proteins. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria . PQQC has been found to be required in the synthesis of PQQ but its function is unclear. The exact molecular function of members of this family is uncertain.
Pang AS, Nathoo S, Wong SL; , J Bacteriol 1991;173:46-54.: Cloning and characterization of a pair of novel genes that regulate production of extracellular enzymes in Bacillus subtilis. PUBMED:1898926 EPMC:1898926
Toyama H, Fukumoto H, Saeki M, Matsushita K, Adachi O, Lidstrom ME; , Biochem Biophys Res Commun 2002;299:268-272.: PqqC/D, which converts a biosynthetic intermediate to pyrroloquinoline quinone. PUBMED:12437981 EPMC:12437981
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR004305
Proteins containing this domain are found in all the three major phyla of life: archaebacteria, eubacteria, and eukaryotes. In Bacillus subtilis, TenA is one of a number of proteins that enhance the expression of extracellular enzymes, such as alkaline protease, neutral protease and levansucrase [PUBMED:1898926] and has been identified as a Thiaminase 2 [PUBMED:15709744]. The THI-4 protein, which is involved in thiamine biosynthesis, also contains this domain. The C-terminal part of these proteins consistently show significant sequence similarity to TenA proteins. This similarity was first noted with the Neurospora crassa THI-4 [PUBMED:8662211].
This domain is also found in bacterial coenzyme PQQ synthesis protein C or PQQC. Pyrroloquinoline quinone (PQQ) is the prosthetic group of several bacterial enzymes,including methanol dehydrogenase of methylotrophs and the glucose dehydrogenase of a number of bacteria [PUBMED:12437981]. PQQC has been found to be required in the synthesis of PQQ, but its function is unclear.
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This clan includes the Heme oxygenase family as well as the TENA/THI-4/PQQC family that are less well characterised .
The clan contains the following 5 members:DUF3050 DUF3865 Haem_oxygenas_2 Heme_oxygenase TENA_THI-4
We make a range of alignments for each Pfam-A family:
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Curation and family details
|Seed source:||Pfam-B_2039 (release 6.4) & Pfam-B_7791 (release 7.7)|
|Number in seed:||25|
|Number in full:||3227|
|Average length of the domain:||201.20 aa|
|Average identity of full alignment:||20 %|
|Average coverage of the sequence by the domain:||78.91 %|
|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:||11|
|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 TENA_THI-4 domain has been found. There are 70 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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