| Basic Information | |
|---|---|
| Species | Selaginella moellendorffii |
| Cazyme ID | 404365 |
| Family | AA7 |
| Protein Properties | Length: 402 Molecular Weight: 42937.5 Isoelectric Point: 7.5288 |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 28 | 179 | 1.1e-30 |
| VTVGAGVKWEELYQAVFDRKFVLVGGGSSSVGAAGGHPQGGGRSPLSPTFGLAADNVLEFSVVTSDGSLAVANRCQNQHLYWAMRGGGGGGGTFGIAATH WLYPALDSLVFAQYNLSTPDKPSFQRTLAQFTELHPSLERAGWAGTFLITNT | |||
| Full Sequence |
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| Protein Sequence Length: 402 Download |
| MKSMRFHHRF LPSGCSHRSK GATYLPAVTV GAGVKWEELY QAVFDRKFVL VGGGSSSVGA 60 AGGHPQGGGR SPLSPTFGLA ADNVLEFSVV TSDGSLAVAN RCQNQHLYWA MRGGGGGGGT 120 FGIAATHWLY PALDSLVFAQ YNLSTPDKPS FQRTLAQFTE LHPSLERAGW AGTFLITNTT 180 ELTLSYLLPN SGMELASATL GAPLEELARE DPQLRSSGSL QSFPSFQEFR LAIQCQGRSS 240 CRDVDTATTA GIPLASRRIP RTTVAYSPGN LAEAMVRIRE LFPRVSLTGV FVGGGAVSRD 300 GRDNAVNPAW RRVLWHVMAE LSAANAILVD LTPGSGAYGN EADFDEAQWP VCVEICMKGV 360 GERKSDEGNG MTIAKEQEEI QASGGEWKAQ CTPKHAKIQK V* 420 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 0.005 | 28 | 321 | 311 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 0.0009 | 28 | 96 | 70 | + FAD binding domain. This family consists of various enzymes that use FAD as a co-factor, most of the enzymes are similar to oxygen oxidoreductase. One of the enzymes Vanillyl-alcohol oxidase (VAO) has a solved structure, the alignment includes the FAD binding site, called the PP-loop, between residues 99-110. The FAD molecule is covalently bound in the known structure, however the residue that links to the FAD is not in the alignment. VAO catalyzes the oxidation of a wide variety of substrates, ranging form aromatic amines to 4-alkylphenols. Other members of this family include D-lactate dehydrogenase, this enzyme catalyzes the conversion of D-lactate to pyruvate using FAD as a co-factor; mitomycin radical oxidase, this enzyme oxidises the reduced form of mitomycins and is involved in mitomycin resistance. This family includes MurB an UDP-N-acetylenolpyruvoylglucosamine reductase enzyme EC:1.1.1.158. This enzyme is involved in the biosynthesis of peptidoglycan. | ||
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2bvh_D | 0.0007 | 30 | 115 | 105 | 189 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2bvh_C | 0.0007 | 30 | 115 | 105 | 189 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2bvh_B | 0.0007 | 30 | 115 | 105 | 189 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2bvh_A | 0.0007 | 30 | 115 | 105 | 189 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| PDB | 2bvg_D | 0.0007 | 30 | 115 | 105 | 189 | A Chain A, Crystal Structure Of Galactose Oxidase Mutant W290f |
| Hydropathy |
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| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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