Summary
2OG-Fe(II) oxygenase superfamily
This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily [1]. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity EC:1.14.11.2 catalysing the reaction: Procollagen L-proline + 2-oxoglutarate + O2 <=> procollagen trans- 4-hydroxy-L-proline + succinate + CO2. The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site [3]. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.
Literature references
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Aravind L, Koonin EV; , Genome Biol 2001;2:RESEARCH0007.: The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases. PUBMED:11276424
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Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI; , J Biol Chem 1997;272:17342-17348.: Cloning of the human prolyl 4-hydroxylase alpha subunit isoform alpha(II) and characterization of the type II enzyme tetramer. The alpha(I) and alpha(II) subunits do not form a mixed alpha(I)alpha(II)beta2 tetramer. PUBMED:9211872
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Helaakoski T, Annunen P, Vuori K, MacNeil IA, Pihlajaniemi T, Kivirikko KI; , Proc Natl Acad Sci U S A 1995;92:4427-4431.: Cloning, baculovirus expression, and characterization of a second mouse prolyl 4-hydroxylase alpha-subunit isoform: formation of an alpha 2 beta 2 tetramer with the protein disulfide-isomerase/beta subunit. PUBMED:7753822
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Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE; , Nature 1995;375:700-704.: Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. PUBMED:7791906
InterPro entry IPR005123
This family contains members of the 2-oxoglutarate (2OG) and Fe(II)-dependent oxygenase superfamily PUBMED:11276424. This family includes the C-terminal of prolyl 4-hydroxylase alpha subunit. The holoenzyme has the activity () catalysing the reaction:
The full enzyme consists of a alpha2 beta2 complex with the alpha subunit contributing most of the parts of the active site PUBMED:7753822. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.
Clan
This family is a member of clan Cupin (CL0029), which contains the following 35 members:
2OG-FeII_Oxy 3-HAO AraC_binding AraC_N ARD Asp_Arg_Hydrox Auxin_BP CDO_I CsiD Cupin_1 Cupin_2 Cupin_3 Cupin_4 Cupin_5 dTDP_sugar_isom DUF1255 DUF1479 DUF1498 DUF1637 DUF1971 DUF386 Ectoine_synth EutQ FdtA GPI HgmA JmjC KduI MannoseP_isomer Mif2 PhyH Pirin Pirin_C PMI_typeI TauDGene Ontology
| Molecular function | oxidoreductase activity (GO:0016491) |
External database links
| PANDIT: | PF03171 |
| PROSITE: | PDOC01028 PDOC00165 |
| SCOP: | 1ips |
| SYSTERS: | 2OG-FeII_Oxy |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Alignments
There are various ways to view or download the sequence alignments that we store. You can use a sequence viewer to look at either the seed or full alignment for the family, or you can look at a plain text version of the sequence in a variety of different formats. More...
View options
Formatting options
Download options
Very large alignments can often cause problems for the formatting tool above. If you find that downloading or viewing a large alignment is problematic, you can also download a gzip-compressed, Stockholm-format file containing the seed or full alignment for this family.
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
The main seed and full alignments are generated using sequences from the UniProt sequence database. However, we also generate alignments using sequences from the NCBI sequence database and the "metaseq" metagenomics dataset.
You can view alignments from these two additional datasets using the form above, or you can download alignments of NCBI or metagenomics sequences, as gzip-compressed files.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER2.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family. 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 or full alignments.
Note: You can also download the data files for the seed, full, NCBI or metagenomics trees.
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: | Aravind L |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Aravind L |
| Number in seed: | 139 |
| Number in full: | 5362 |
| Average length of the domain: | 102.70 aa |
| Average identity of full alignment: | 22 % |
| Average coverage of the sequence by the domain: | 29.71 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 9421015 -E 1000 HMM pfamseq
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| Model details: |
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| Model length: | 97 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
Tree controls
HideThe tree shows the occurrence of this domain across different species. More...
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Interactions
There is 1 interaction for this family. More...
2OG-FeII_OxyStructures
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 2OG-FeII_Oxy domain has been found.
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