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InterPro: IPR006638 Elongator protein 3/MiaB/NifB
Protein matches
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UniProtKB Matches: 22157 proteins |
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Accession
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IPR006638 Elp3/MiaB/NifB |
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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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Parent
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IPR007197 Radical SAM
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Children
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IPR003698 Lipoate synthase
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Found in
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IPR002684 Biotin synthase
IPR004383 Ribosomal RNA large subunit methyltransferase RlmN;
IPR004558 Oxygen-independent coproporphyrinogen III oxidase HemN
IPR005244 FO synthase, subunit 2-like
IPR005839 Methylthiotransferase
IPR005840 Ribosomal protein S12 methylthiotransferase RimO
IPR005909 Conserved hypothetical protein CHP01210
IPR005910 Histone acetyltransferase ELP3
IPR005911 Conserved hypothetical protein CHP01212
IPR006463 tRNA-i(6)A37 modification enzyme MiaB
IPR006466 MiaB-like tRNA modifying enzyme, archaeal-type
IPR006467 MiaB-like tRNA modifying enzyme
IPR011772 Magnesium-protoporphyrin IX monomethyl ester anaerobic oxidative cyclase
IPR011843 Coenzyme PQQ biosynthesis protein E, bacteria
IPR013483 Molybdenum cofactor biosynthesis protein A
IPR013485 Molybdenum cofactor biosynthesis protein A, archaea
IPR013785 Aldolase-type TIM barrel
IPR014494 Predicted Fe-S oxidoreductase, NifB/MoaA-like family, euryarchaeota type
IPR016431 Pyruvate-formate lyase-activating enzyme, predicted
IPR016779 Radical SAM enzyme, bacteria, predicted
IPR017200 Coenzyme PQQ biosynthesis protein E
IPR017672 Putative methanogenesis marker protein 10
IPR017833 Hopanoid biosynthesis associated radical SAM protein HpnH
IPR017834 Hopanoid biosynthesis associated radical SAM protein HpnJ
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
IPR020612 Methylthiotransferase, conserved site
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InterPro annotation
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 Entry Details in BioMart
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Abstract
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This domain is found in MoaA, NifB, PqqE, coproporphyrinogen
III oxidase, biotin synthase
and MiaB families, and includes a representative in the eukaryotic elongator
subunit, Elp-3. Some
members of the family are methyltransferases [1].
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Structural links
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Database links
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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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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 2001 1097-106
[PubMed: 11222759]
http://dx.doi.org/10.1093/nar/29.5.1097
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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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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 2004 12870-5
[PubMed: 15317939]
http://dx.doi.org/10.1073/pnas.0404624101
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InterPro 23.1
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