Summary: PQQ enzyme repeat
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PQQ enzyme repeat Provide feedback
The family represent a single repeat of a beta propeller. This propeller has been found in several enzymes which utilise pyrrolo-quinoline quinone as a prosthetic group.
Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C; , Structure 1995;3:177-187.: The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A. PUBMED:7735834 EPMC:7735834
Xia Z, Dai W, Zhang Y, White SA, Boyd GD, Mathews FS; , J Mol Biol 1996;259:480-501.: Determination of the gene sequence and the three-dimensional structure at 2.4 angstroms resolution of methanol dehydrogenase from Methylophilus W3A1. PUBMED:8676383 EPMC:8676383
Internal database links
|SCOOP:||Neisseria_PilC PQQ_2 PQQ_3 SUKH-4 DUF4905|
|Similarity to PfamA using HHSearch:||PQQ_2 PQQ_2 PQQ_3|
External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR002372Pyrrolo-quinoline quinone (PQQ) is a redox coenzyme, which serves as a cofactor for a number of enzymes (quinoproteins) and particularly for some bacterial dehydrogenases [PUBMED:2549854, PUBMED:2572081]. A number of bacterial quinoproteins belong to this family.
Enzymes in this group have repeats of a beta propeller.
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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 large clan contains proteins that contain beta propellers. These are composed of between 6 and 8 repeats. The individual repeats are composed of a four stranded sheet. The clan includes families such as WD40 Pfam:PF00400 where the individual repeats are modeled. The clan also includes families where the entire propeller is modeled such as Pfam:PF02239 usually because the individual repeats are not discernible. These proteins carry out a very wide diversity of functions including catalysis.
The clan contains the following 70 members:ANAPC4_WD40 Arylesterase Arylsulfotran_2 Arylsulfotrans BBS2_Mid Beta_propel Coatomer_WDAD CPSF_A Cytochrom_D1 DPPIV_N DUF1513 DUF1668 DUF2415 DUF3312 DUF4221 DUF4934 DUF5050 DUF5122 DUF5128 DUF839 eIF2A FG-GAP FG-GAP_2 Ge1_WD40 Glu_cyclase_2 Gmad1 GSDH IKI3 Itfg2 Kelch_1 Kelch_2 Kelch_3 Kelch_4 Kelch_5 Kelch_6 Lactonase Ldl_recept_b Lgl_C LVIVD Me-amine-dh_H MRJP Nbas_N Neisseria_PilC NHL Nucleoporin_N Nup160 PALB2_WD40 PD40 Pectate_lyase22 Peptidase_S9_N Phytase-like PQQ PQQ_2 PQQ_3 RAG2 RCC1 RCC1_2 Reg_prop SBBP SBP56 SdiA-regulated SGL Str_synth TcdB_toxin_midN TolB_like VCBS WD40 WD40_3 WD40_4 WD40_like
We make a range of alignments for each Pfam-A family:
- the curated alignment from which the HMM for the family is built
- the alignment generated by searching the sequence database using the HMM
- Representative Proteomes (RPs) at 15%, 35%, 55% and 75% co-membership thresholds
- alignment generated by searching the UniProtKB sequence database using the family HMM
- 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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Curation and family details
|Seed source:||Pfam-B_1319 (release 3.0)|
|Number in seed:||71|
|Number in full:||992|
|Average length of the domain:||36.00 aa|
|Average identity of full alignment:||25 %|
|Average coverage of the sequence by the domain:||8.13 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 11927849 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||18|
|Download:||download the raw HMM for this family|
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There are 5 interactions 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 PQQ domain has been found. There are 86 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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