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Basic Information | |
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Species | Manihot esculenta |
Cazyme ID | cassava4.1_022715m |
Family | AA7 |
Protein Properties | Length: 551 Molecular Weight: 60777.2 Isoelectric Point: 7.1148 |
Chromosome | Chromosome/Scaffold: 06700 Start: 283671 End: 285323 |
Description | FAD-binding Berberine family protein |
View CDS |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 70 | 532 | 0 |
AEPTIPKPLAIVQPESVDQLVKTVTCCREGLLEIRVRCGGHSYEGTSSVASDGAPFIIIDMMNLNKVSVELEGEVAFVEGGATLGETYSAIAEASSVHGF SAGSCPTVGVGGHIGGGGFGLLSRKYGLAADNVVDALLVDARGRLLDRKAMGEDVFWAIRGGGGGVWGIVYAWKIKLLKVPQVVTCFTVSRPGTKTHVAK LINKWQYVAPRLDGDFYVSCFVGAGLPETKTPGISATFKGFFLGPRNEAMAILNKIFPELGILEEDCKEMSWIESILFFSGLSKGSSVSDLKNRYLQGKQ YFKAKSDYVKREISLAGINGALDILEKEPKGYVILDPYGGMMDKISGEAIAFPHRKGNLFAIQYMVEWKEKDNNKSKEYIDWVREFYNSMTPFASWGPRA AYINYMDFDLGVMKMLKMRVPSRDAVEAARVWGEKYFLKNFDRLVRAKTIIDPDNVFSNLQSI |
Full Sequence |
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Protein Sequence Length: 551 Download |
MVNFLPAIPS FLFIFIFFLL APPLCALHDQ LTSCLSYNHI TNFTFFPSTE NDSTAYFNLL 60 EFSIQNLRFA EPTIPKPLAI VQPESVDQLV KTVTCCREGL LEIRVRCGGH SYEGTSSVAS 120 DGAPFIIIDM MNLNKVSVEL EGEVAFVEGG ATLGETYSAI AEASSVHGFS AGSCPTVGVG 180 GHIGGGGFGL LSRKYGLAAD NVVDALLVDA RGRLLDRKAM GEDVFWAIRG GGGGVWGIVY 240 AWKIKLLKVP QVVTCFTVSR PGTKTHVAKL INKWQYVAPR LDGDFYVSCF VGAGLPETKT 300 PGISATFKGF FLGPRNEAMA ILNKIFPELG ILEEDCKEMS WIESILFFSG LSKGSSVSDL 360 KNRYLQGKQY FKAKSDYVKR EISLAGINGA LDILEKEPKG YVILDPYGGM MDKISGEAIA 420 FPHRKGNLFA IQYMVEWKEK DNNKSKEYID WVREFYNSMT PFASWGPRAA YINYMDFDLG 480 VMKMLKMRVP SRDAVEAARV WGEKYFLKNF DRLVRAKTII DPDNVFSNLQ SIPPMPSSVG 540 SKATVKEDML * 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 5.0e-15 | 470 | 533 | 64 | + 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 | 8.0e-16 | 77 | 534 | 471 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 4.0e-23 | 77 | 216 | 141 | + 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. |
Gene Ontology | |
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GO Term | Description |
GO:0008762 | UDP-N-acetylmuramate dehydrogenase activity |
GO:0016491 | oxidoreductase activity |
GO:0050660 | flavin adenine dinucleotide binding |
GO:0055114 | oxidation-reduction process |
Annotations - NR Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
EMBL | CBI16966.1 | 0 | 1 | 538 | 277 | 770 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 0 | 373 | 513 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 11 | 535 | 12 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 17 | 541 | 3 | 532 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 1 | 545 | 1 | 546 | 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 | 535 | 7 | 519 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3d2h_A | 0 | 16 | 535 | 7 | 519 | A Chain A, Solution Structure Of The C-Terminal Domain Ole E 9 |
PDB | 3d2d_A | 0 | 16 | 535 | 7 | 519 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 31 | 535 | 2 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 29 | 535 | 6 | 500 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |