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InterPro: IPR007197 Radical SAM
Protein matches
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UniProtKB Matches: 28359 proteins |
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Accession
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IPR007197 Radical_SAM |
Type
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Domain |
Signatures
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InterPro Relationships
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Children
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IPR006638 Elongator protein 3/MiaB/NifB
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Found in
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IPR003739 Protein of unknown function DUF160
IPR004383 Ribosomal RNA large subunit methyltransferase RlmN;
IPR011352 Pyruvate formate-lyase 2 activating enzyme
IPR012726 Thiazole biosynthesis ThiH
IPR012837 Ribonucleoside-triphosphate reductase activating, anaerobic
IPR012838 Pyruvate formate-lyase activating
IPR012839 Glycyl radical enzyme-activating
IPR012840 Ribonucleoside-triphosphate reductase, anaerobic-like
IPR016771 Fe-S oxidoreductase, radical SAM domain-containing, TM0948, predicted
IPR016863 Reductase, EryCV, predicted
IPR017742 7-cyano-7-deazaguanosine (preQ0) biosynthesis protein QueE
IPR019939 FO synthase, subunit 1
IPR019940 Complex F420, CofH
IPR020050 FO synthase, subunit 2
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Contains
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IPR000385 MoaA/nifB/pqqE, iron-sulphur binding, conserved site
IPR001989 Radical-activating enzyme, conserved site
IPR020612 Methylthiotransferase, conserved site
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GO Term annotation
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Function
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GO:0003824 catalytic activity
GO:0051536 iron-sulfur cluster binding
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InterPro annotation
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Entry Details in BioMart
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Abstract
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Radical SAM proteins catalyze diverse reactions, including unusual methylations, isomerization, sulphur insertion, ring formation, anaerobic oxidation and protein radical formation. Evidence exists that these proteins generate a radical species by reductive cleavage of S:-adenosylmethionine (SAM) through an unusual Fe-S centre [1, 2].
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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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Sofia HJ, Chen G, Hetzler BG, Reyes-Spindola JF, Miller NE.
Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods.
Nucleic Acids Res. 29 1097-106 2001
[PubMed: 11222759]
http://dx.doi.org/10.1093/nar/29.5.1097
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2.
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Hanzelmann P, Schindelin H.
Crystal structure of the S-adenosylmethionine-dependent enzyme MoaA and its implications for molybdenum cofactor deficiency in humans.
Proc. Natl. Acad. Sci. U.S.A. 101 12870-5 2004
[PubMed: 15317939]
http://dx.doi.org/10.1073/pnas.0404624101
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Additional Reading
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Berkovitch F, Nicolet Y, Wan JT, Jarrett JT, Drennan CL.
Crystal structure of biotin synthase, an S-adenosylmethionine-dependent radical enzyme.
Science 303 2004 76-9
[PubMed: 14704425]
http://dx.doi.org/10.1126/science.1088493
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Layer G, Moser J, Heinz DW, Jahn D, Schubert WD.
Crystal structure of coproporphyrinogen III oxidase reveals cofactor geometry of Radical SAM enzymes.
EMBO J. 22 2003 6214-24
[PubMed: 14633981]
http://dx.doi.org/10.1093/emboj/cdg598
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Berteau O, Guillot A, Benjdia A, Rabot S.
A new type of bacterial sulfatase reveals a novel maturation pathway in prokaryotes.
J. Biol. Chem. 281 2006 22464-70
[PubMed: 16766528]
http://dx.doi.org/10.1074/jbc.M602504200
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Benjdia A, Leprince J, Guillot A, Vaudry H, Rabot S, Berteau O.
Anaerobic sulfatase-maturating enzymes: radical SAM enzymes able to catalyze in vitro sulfatase post-translational modification.
J. Am. Chem. Soc. 129 2007 3462-3
[PubMed: 17335281]
http://dx.doi.org/10.1021/ja067175e
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Hanzelmann P, Schindelin H.
Binding of 5'-GTP to the C-terminal FeS cluster of the radical S-adenosylmethionine enzyme MoaA provides insights into its mechanism.
Proc. Natl. Acad. Sci. U.S.A. 103 2006 6829-34
[PubMed: 16632608]
http://dx.doi.org/10.1073/pnas.0510711103
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InterPro 23.1
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