Basic Information | |
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Species | Gossypium raimondii |
Cazyme ID | Gorai.001G069600.1 |
Family | AA7 |
Protein Properties | Length: 542 Molecular Weight: 60001.5 Isoelectric Point: 6.7489 |
Chromosome | Chromosome/Scaffold: 01 Start: 7017195 End: 7018820 |
Description | FAD-binding Berberine family protein |
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 | 66 | 528 | 0 |
AEPTIPKPIAIILPENKEQLINTVVCCTKGPWEIRVRCGGHSYEGTSSVASDGAPFVIIDMMNLNRVSVDLGNETAWVEGGATLGETYHAIAESSFIHGF AAGSCPTVGTGGHIGGGGFGFLSRKYGLAADNVIDALLLNAEGELLDRQAMGEDVFWAIRGGGGGIWGIVYAWKIKLLRVPKTVTSFIVSRPGTKAHVAN LVNKWQHVAPNLEGDMYLSCAVGAGLPQAKSIGISATFNGFFLGRKREAVLILRRVFAELGVAEEDCKEMSWIESVLFFSGLGDGALVSDLKNRYLHDKH YFKAKSDYVRNPISLTGIRTAIDILEKQPRGYIIMDPYGGIMNNISNDSIAFPHRYGNLYTIQYLVEWHQEEKNRSNEYREWIRDFYDAMASHVSWGPRA AYVNYMDFDLGVMELINTSVLSEDTVEMARVWGEKYFLNNYDRLVKAKTLIDPNNVFKNQQGI |
Full Sequence |
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Protein Sequence Length: 542 Download |
MVNLSLLLLH FLISSLSVSG SAATDQRNIM SCLNYYNISN YTISSNVHNH DYSILLNFSI 60 QNLRFAEPTI PKPIAIILPE NKEQLINTVV CCTKGPWEIR VRCGGHSYEG TSSVASDGAP 120 FVIIDMMNLN RVSVDLGNET AWVEGGATLG ETYHAIAESS FIHGFAAGSC PTVGTGGHIG 180 GGGFGFLSRK YGLAADNVID ALLLNAEGEL LDRQAMGEDV FWAIRGGGGG IWGIVYAWKI 240 KLLRVPKTVT SFIVSRPGTK AHVANLVNKW QHVAPNLEGD MYLSCAVGAG LPQAKSIGIS 300 ATFNGFFLGR KREAVLILRR VFAELGVAEE DCKEMSWIES VLFFSGLGDG ALVSDLKNRY 360 LHDKHYFKAK SDYVRNPISL TGIRTAIDIL EKQPRGYIIM DPYGGIMNNI SNDSIAFPHR 420 YGNLYTIQYL VEWHQEEKNR SNEYREWIRD FYDAMASHVS WGPRAAYVNY MDFDLGVMEL 480 INTSVLSEDT VEMARVWGEK YFLNNYDRLV KAKTLIDPNN VFKNQQGIPP STTIGLKART 540 F* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
TIGR01679 | bact_FAD_ox | 0.002 | 73 | 158 | 87 | + FAD-linked oxidoreductase. This model represents a family of bacterial oxidoreductases with covalently linked FAD, closely related to two different eukaryotic oxidases, 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. | ||
COG0277 | GlcD | 2.0e-13 | 73 | 522 | 464 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 3.0e-15 | 466 | 529 | 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. | ||
pfam01565 | FAD_binding_4 | 1.0e-23 | 73 | 212 | 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 | 11 | 540 | 288 | 776 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 0 | 369 | 509 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 3 | 537 | 7 | 540 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 21 | 539 | 9 | 534 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 7 | 530 | 14 | 534 | 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 | 3fw9_A | 0 | 28 | 530 | 1 | 493 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 28 | 541 | 7 | 510 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 28 | 541 | 7 | 510 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 28 | 541 | 26 | 529 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 28 | 541 | 26 | 529 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |