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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 229910 |
Family | AA7 |
Protein Properties | Length: 562 Molecular Weight: 60381.9 Isoelectric Point: 6.7122 |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 110 | 306 | 0 |
NVSSASHVQRAVEFAATYNLRVTVKNTGHDYLGRSNAAGSLSIWTHHLKDISFVEEFVPEGCNSSAARSGVTIGAGVVWEELYRAADAHGKAIAGAQCSS VGAAGGYPQAAGHSPLSPKYGLSADNVLQYKVVTADGKLVVANACQNKDLFWALRGGGGGTFGVVVSVTHATHPALKSLQFASYVVGANTSESFELV |
Full Sequence |
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Protein Sequence Length: 562 Download |
MRARPTAFSC KCLPSDDCWP DSSAWQALNA SIDGQLVASK PPAWPCHEPE YNALQCLEVT 60 QKWSDAFWRA AQPGAMQDSF FEMDGNEGCL LSGNKTSSCY QGRVSVFAVN VSSASHVQRA 120 VEFAATYNLR VTVKNTGHDY LGRSNAAGSL SIWTHHLKDI SFVEEFVPEG CNSSAARSGV 180 TIGAGVVWEE LYRAADAHGK AIAGAQCSSV GAAGGYPQAA GHSPLSPKYG LSADNVLQYK 240 VVTADGKLVV ANACQNKDLF WALRGGGGGT FGVVVSVTHA THPALKSLQF ASYVVGANTS 300 ESFELVVTEF VKSNPGLSQD GWGGFFLIAK RALIVQYLLP DKNSSFAQSS FDPFLSEARG 360 IAGVSVNGAM QSFSSYLKWH EAVQCSKSGC SFATGSSELL VSRLIPSSTF SDDPEELAQT 420 LVGIWDEGYD RVMGYLTAGG EVSVARDNAV NPAWREALWH IIVVKLFPAN ETQAAKKSLA 480 RAITKTGGRL RRVAPSSGCY LNEADVNEPD WQQAFFGDKY DKLKLIKEAV DPQGLFVCKK 540 CVGSEDWSED LTCRSKKKCR A* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 2.0e-9 | 499 | 536 | 38 | + Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine. | ||
COG0277 | GlcD | 2.0e-13 | 118 | 536 | 434 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 4.0e-15 | 118 | 252 | 136 | + 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3tsj_B | 0.00000000001 | 106 | 276 | 54 | 217 | A Chain A, Polygalacturonase From Erwinia Carotovora Ssp. Carotovora |
PDB | 3tsj_A | 0.00000000001 | 106 | 276 | 54 | 217 | A Chain A, Polygalacturonase From Erwinia Carotovora Ssp. Carotovora |
PDB | 3tsh_A | 0.00000000001 | 106 | 276 | 54 | 217 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_D | 0.00000000002 | 113 | 277 | 47 | 198 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 2bvh_C | 0.00000000002 | 113 | 277 | 47 | 198 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Sequence Alignments (This image is cropped. Click for full image.) |
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