Basic Information | |
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Species | Picea abies |
Cazyme ID | MA_162773g0010 |
Family | AA7 |
Protein Properties | Length: 518 Molecular Weight: 57571.7 Isoelectric Point: 8.6189 |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 62 | 514 | 0 |
QNLRYTESSVRKPYALIVPRSRQEVQKSVACCIRHGWEIRVRSGGHSYEGLSSTSDIPFVIVDLMNLDAININMASKTAWVEAGATVGQLYDAIADRTEI YGFSAGSCTTMGTGGHFSGGGLGLLSRKYGVAADNIIDALLVDARGNLLNRKKMGEDVFWALRGGGGGSWGVMVAWRIKLVRVPPVVTVFTVARKGRDAV TKLVHRWQSIAPVVEEDLYMNAVVSGTQVKGGTRDVEVTFGGMYLGPLDQLLKTVNKSFPELGMGSSDCKEMSWIDSISNTAFTNRTELRNRYNAGKNYF KAKSDFVRSPITPSALHGAWKFLEEELKCYVILDPLGGIMDKIRSSEIPFPHRAGNLYMIQYQITWNDPSKDAEYIASIRRFYEYMTPYVSDSPRAAYVN YQDLDLGVDPNGTATVEEARSWGEKYFVHNYDRLVKVKSTIDPYNVYRNSQSI |
Full Sequence |
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Protein Sequence Length: 518 Download |
MAVLGYLKWI SVCFLIFCQL VVASISGQDG LITCLERNAV RNVTTSASSS TEYYSLLNFS 60 VQNLRYTESS VRKPYALIVP RSRQEVQKSV ACCIRHGWEI RVRSGGHSYE GLSSTSDIPF 120 VIVDLMNLDA ININMASKTA WVEAGATVGQ LYDAIADRTE IYGFSAGSCT TMGTGGHFSG 180 GGLGLLSRKY GVAADNIIDA LLVDARGNLL NRKKMGEDVF WALRGGGGGS WGVMVAWRIK 240 LVRVPPVVTV FTVARKGRDA VTKLVHRWQS IAPVVEEDLY MNAVVSGTQV KGGTRDVEVT 300 FGGMYLGPLD QLLKTVNKSF PELGMGSSDC KEMSWIDSIS NTAFTNRTEL RNRYNAGKNY 360 FKAKSDFVRS PITPSALHGA WKFLEEELKC YVILDPLGGI MDKIRSSEIP FPHRAGNLYM 420 IQYQITWNDP SKDAEYIASI RRFYEYMTPY VSDSPRAAYV NYQDLDLGVD PNGTATVEEA 480 RSWGEKYFVH NYDRLVKVKS TIDPYNVYRN SQSIPVNK |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 2.0e-13 | 458 | 515 | 58 | + 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-20 | 72 | 515 | 466 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 9.0e-23 | 74 | 211 | 139 | + 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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
RefSeq | XP_002264336.1 | 0 | 4 | 515 | 5 | 532 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268361.1 | 0 | 14 | 515 | 9 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002277281.1 | 0 | 11 | 515 | 6 | 526 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 20 | 515 | 5 | 524 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 10 | 515 | 14 | 533 | d-lactate dehydrogenase, putative [Ricinus communis] |
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 | 3d2j_A | 0 | 16 | 515 | 13 | 517 | A Chain A, Peanut Peroxidase |
PDB | 3d2h_A | 0 | 16 | 515 | 13 | 517 | A Chain A, Peanut Peroxidase |
PDB | 3d2d_A | 0 | 16 | 515 | 13 | 517 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 31 | 515 | 2 | 492 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 26 | 515 | 4 | 498 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |