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Prior-Knowledge Description Expectation Prediction Conclusion Leaf Statistics
GenProp0860 tryptophan tryptophylquinone modification of methylamine dehydrogenase~The maturation enzyme MauG completes the modification and cross-linking of a pair of Trp residues into the novel cofactor tryptophan tryptophylquinone, or TTQ, in the light chain (MauA) of methylamine dehydrogenase. While some analogous enzyme cofactors are produced autocatalytically from amino acids in the precursor polypeptide, TTQ is produced with aid of the maturation enzyme MauG. MauG is a di-heme enzyme with peroxidase activity, similar to di-heme cytochrome c peroxidases of other biological systems. Interestingly, the pair of modified Trp residues is conserved in MauA homologs in species that have no MauG homolog in the vicinity, suggesting no modification, autocatalytic modification, or a different modification enzyme. None - {{∅}} None - {{∅}} Unexplained
Evidence_85700 TIGR02658 HMM None - {{∅}} None - {{∅}} Unexplained
Component_63056 methylamine dehydrogenase, light chain None - {{∅}} None - {{∅}} Unexplained
Evidence_85699 TIGR02661 HMM None - {{∅}} None - {{∅}} Unexplained
Evidence_85698 TIGR02659 HMM None - {{∅}} None - {{∅}} Unexplained
Component_63948 methylamine dehydrogenase heavy chain None - {{∅}} None - {{∅}} Unexplained
Evidence_85697 TIGR03791 HMM None - {{∅}} None - {{∅}} Unexplained
Component_63947 methylamine dehydrogenase accessory protein MauD None - {{∅}} None - {{∅}} Unexplained
Component_63057 TTQ maturation di-heme protein MauG None - {{∅}} None - {{∅}} Unexplained