| Basic Information | |
|---|---|
| Species | Picea abies |
| Cazyme ID | MA_10427412g0010 |
| Family | AA7 |
| Protein Properties | Length: 492 Molecular Weight: 53205.6 Isoelectric Point: 7.0331 |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA7 | 57 | 194 | 0 |
| VSKPYVIVIPQNKEQVKNSVVCCVKNGWEIRVRSGGHSYEGLSYTSDVPFVLIDLMNFDNVHVDTESMTAWVEAGATLGQVYYGIANKTNNHGFPAGICP TVGSGGHIAGGGLSFLSRKYGVAADNVIDALLVNASVT | |||
| AA7 | 242 | 461 | 0 |
| FAEPGVRKPYVIVIPQSKEQVKNSVVCCVKNRWEIRVRSGGHSYEGLSYTSDVPFVLIDLMNFDNVHVDIKSMTAWVEAGATLGQVYSGIANKTNNNGFP AGTCPTIGSGGHFAGGGLGFLSRKYGLAADNVIDALLVNASGEIMDKKAMGDDVFWALRGGGGGSWGVVIAWKIKLVSVPTILTAFVVSRTGRDVVTGII HRWQYIWPFVEEDLFMRVQF | |||
| Full Sequence |
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| Protein Sequence Length: 492 Download |
| MAVTNARDAP DPAAGLISCL HDLDLKNITT MSSSSTSEYD VLLNFSLQNL RFAEPGVSKP 60 YVIVIPQNKE QVKNSVVCCV KNGWEIRVRS GGHSYEGLSY TSDVPFVLID LMNFDNVHVD 120 TESMTAWVEA GATLGQVYYG IANKTNNHGF PAGICPTVGS GGHIAGGGLS FLSRKYGVAA 180 DNVIDALLVN ASVTNARDAP DPGAGLISCL HDRRLKNITT MSSSSTSEYD VLLNFSLQNL 240 RFAEPGVRKP YVIVIPQSKE QVKNSVVCCV KNRWEIRVRS GGHSYEGLSY TSDVPFVLID 300 LMNFDNVHVD IKSMTAWVEA GATLGQVYSG IANKTNNNGF PAGTCPTIGS GGHFAGGGLG 360 FLSRKYGLAA DNVIDALLVN ASGEIMDKKA MGDDVFWALR GGGGGSWGVV IAWKIKLVSV 420 PTILTAFVVS RTGRDVVTGI IHRWQYIWPF VEEDLFMRVQ FFGITVEGGT KKDMNASFQG 480 MYLGRKEQFL KI |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01678 | FAD_lactone_ox | 0.008 | 249 | 462 | 219 | + sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1. | ||
| COG0277 | GlcD | 1.0e-12 | 60 | 191 | 139 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| COG0277 | GlcD | 9.0e-16 | 248 | 444 | 207 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 5.0e-20 | 60 | 192 | 134 | + 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. | ||
| pfam01565 | FAD_binding_4 | 5.0e-21 | 250 | 385 | 137 | + 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 - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| GenBank | AAU20769.1 | 0 | 206 | 487 | 23 | 301 | berberine bridge enzyme [Thalictrum flavum subsp. glaucum] |
| Swiss-Prot | P93479 | 0 | 16 | 192 | 31 | 207 | RETO_PAPSO RecName: Full=Reticuline oxidase; AltName: Full=Berberine bridge-forming enzyme; Short=BBE; AltName: Full=Tetrahydroprotoberberine synthase; Flags: Precursor |
| Swiss-Prot | P93479 | 0 | 206 | 487 | 31 | 307 | RETO_PAPSO RecName: Full=Reticuline oxidase; AltName: Full=Berberine bridge-forming enzyme; Short=BBE; AltName: Full=Tetrahydroprotoberberine synthase; Flags: Precursor |
| RefSeq | XP_002264336.1 | 0 | 11 | 191 | 26 | 210 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002264336.1 | 0 | 201 | 492 | 26 | 321 | PREDICTED: hypothetical protein [Vitis vinifera] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4ec3_A | 0 | 201 | 486 | 3 | 283 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 4ec3_A | 0 | 16 | 192 | 8 | 184 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 201 | 486 | 3 | 283 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3gsy_A | 0 | 16 | 192 | 8 | 184 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2j_A | 0 | 186 | 486 | 10 | 302 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| Hydropathy |
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| EST Download unfiltered results here | ||||
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| Hit | Length | Start | End | EValue |
| GE476590 | 287 | 205 | 491 | 0 |
| GE476590 | 177 | 15 | 191 | 0 |
| CO481023 | 280 | 205 | 484 | 0 |
| CO481023 | 177 | 15 | 191 | 0 |
| DT631912 | 257 | 182 | 438 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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