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InterPro: IPR005123 Oxoglutarate/iron-dependent oxygenase
Protein matches
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UniProtKB Matches: 6171 proteins |
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Accession
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IPR005123 Oxoglutarate/Fe-dep_oxygenase |
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Type
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Domain |
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Signatures
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InterPro Relationships
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Children
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IPR006620 Prolyl 4-hydroxylase, alpha subunit
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Found in
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IPR002283 Isopenicillin N synthase
IPR004574 Alkylated DNA repair protein AlkB
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Contains
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IPR002057 Isopenicillin N synthase, conserved site
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GO Term annotation
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Function
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GO:0016491 oxidoreductase activity
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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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 [2]. The family also includes lysyl hydrolases, isopenicillin synthases and AlkB.
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Structural links
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Database links
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Publications
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1.
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Aravind L, Koonin EV.
The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases.
Genome Biol. 2 RESEARCH0007 2001
[PubMed: 11276424]
http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=EBI&pubmedid=11276424
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2.
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Helaakoski T, Annunen P, Vuori K, MacNeil IA, Pihlajaniemi T, Kivirikko KI.
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.
Proc. Natl. Acad. Sci. U.S.A. 92 4427-31 1995
[PubMed: 7753822]
http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=7753822&action=stream&blobtype=pdf
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Additional Reading
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Yang CG, Yi C, Duguid EM, Sullivan CT, Jian X, Rice PA, He C.
Crystal structures of DNA/RNA repair enzymes AlkB and ABH2 bound to dsDNA.
Nature 452 2008 961-5
[PubMed: 18432238]
http://dx.doi.org/10.1038/nature06889
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Ge W, Clifton IJ, Stok JE, Adlington RM, Baldwin JE, Rutledge PJ.
Isopenicillin N synthase mediates thiolate oxidation to sulfenate in a depsipeptide substrate analogue: implications for oxygen binding and a link to nitrile hydratase?
J. Am. Chem. Soc. 130 2008 10096-102
[PubMed: 18620394]
http://dx.doi.org/10.1021/ja8005397
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Annunen P, Helaakoski T, Myllyharju J, Veijola J, Pihlajaniemi T, Kivirikko KI.
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.
J. Biol. Chem. 272 1997 17342-8
[PubMed: 9211872]
http://dx.doi.org/10.1074/jbc.272.28.17342
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Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE.
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes.
Nature 375 1995 700-4
[PubMed: 7791906]
http://dx.doi.org/10.1038/375700a0
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Stewart AC, Clifton IJ, Adlington RM, Baldwin JE, Rutledge PJ.
A cyclobutanone analogue mimics penicillin in binding to isopenicillin N synthase.
Chembiochem 8 2007 2003-7
[PubMed: 17907118]
http://dx.doi.org/10.1002/cbic.200700176
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Daruzzaman A, Clifton IJ, Adlington RM, Baldwin JE, Rutledge PJ.
Unexpected oxidation of a depsipeptide substrate analogue in crystalline isopenicillin N synthase.
Chembiochem 7 2006 351-8
[PubMed: 16444759]
http://dx.doi.org/10.1002/cbic.200500282
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Howard-Jones AR, Elkins JM, Clifton IJ, Roach PL, Adlington RM, Baldwin JE, Rutledge PJ.
Interactions of isopenicillin N synthase with cyclopropyl-containing substrate analogues reveal new mechanistic insight.
Biochemistry 46 2007 4755-62
[PubMed: 17397141]
http://dx.doi.org/10.1021/bi062314q
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InterPro 23.1
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