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Basic Information | |
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Species | Carica papaya |
Cazyme ID | evm.model.supercontig_21.234 |
Family | AA7 |
Protein Properties | Length: 549 Molecular Weight: 61266.6 Isoelectric Point: 4.7975 |
Chromosome | Chromosome/Scaffold: 21 Start: 2353869 End: 2355515 |
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 | 56 | 521 | 0 |
ISKPLAIILPESVEEVANSVLCCREASWQIRVRCGGHSYEGTSSVGGDTNKPFVILDMMNLNQVVVDMEDEMAWVEGGATLGEIYYEIAMASQELGFSAG SCPTVGVGGHVTGGGFGFLSRKYGVAADNVVDALLVDSEGELLDRKAMGEDVFWAIRGGGGGVWGVIYAWKIKLLKVPPTVTSFIVSRPESEGFNVAELV EKWQHVAHDLTDDFYLSCFMGAHLPETMTIGMSATFRGFFLGRRTQAISILNKEFPELRVEENDCTDMSWIESVLFFSGLPTGATISELRNRYLQGKGYF KAKSDYVRTPVTFAGIRTMMDILEKEPKGYVIMDPYGGIMKRITSDAIAFPHRKGNLFAIQYLVEWKEEDDEKREDYMDWMRGFYESMKPYVSGGPRAAY VNYMDLDLGQLQPPVSAAIDDLNYSYEDTVEIARVWGEKYFLKNYDRLVRAKTLVDPTNFFTNQQP |
Full Sequence |
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Protein Sequence Length: 549 Download |
MAPSLCTPAD QITYCLNLHN IKNFTTLPNT QNDSNSAYYK LLNFSIQNLR FAGPKISKPL 60 AIILPESVEE VANSVLCCRE ASWQIRVRCG GHSYEGTSSV GGDTNKPFVI LDMMNLNQVV 120 VDMEDEMAWV EGGATLGEIY YEIAMASQEL GFSAGSCPTV GVGGHVTGGG FGFLSRKYGV 180 AADNVVDALL VDSEGELLDR KAMGEDVFWA IRGGGGGVWG VIYAWKIKLL KVPPTVTSFI 240 VSRPESEGFN VAELVEKWQH VAHDLTDDFY LSCFMGAHLP ETMTIGMSAT FRGFFLGRRT 300 QAISILNKEF PELRVEENDC TDMSWIESVL FFSGLPTGAT ISELRNRYLQ GKGYFKAKSD 360 YVRTPVTFAG IRTMMDILEK EPKGYVIMDP YGGIMKRITS DAIAFPHRKG NLFAIQYLVE 420 WKEEDDEKRE DYMDWMRGFY ESMKPYVSGG PRAAYVNYMD LDLGQLQPPV SAAIDDLNYS 480 YEDTVEIARV WGEKYFLKNY DRLVRAKTLV DPTNFFTNQQ PIPPLNMGSS LRKIGSDHGD 540 DHERDKSS* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 8.0e-14 | 59 | 247 | 195 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 3.0e-14 | 454 | 523 | 70 | + 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 | 2.0e-19 | 59 | 199 | 142 | + 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 | 525 | 296 | 767 | unnamed protein product [Vitis vinifera] |
EMBL | CBI16966.1 | 0 | 357 | 503 | 85 | 224 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002264336.1 | 0 | 5 | 525 | 24 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002329230.1 | 0 | 3 | 524 | 8 | 525 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002533924.1 | 0 | 1 | 529 | 20 | 539 | 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 | 4ec3_A | 0 | 10 | 540 | 6 | 516 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 10 | 540 | 6 | 516 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2j_A | 0 | 6 | 540 | 20 | 535 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2h_A | 0 | 6 | 540 | 20 | 535 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
PDB | 3d2d_A | 0 | 6 | 540 | 20 | 535 | A Chain A, Structure Of Berberine Bridge Enzyme 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 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 535 | 3 | 527 | 0 |
GO028240 | 284 | 250 | 533 | 0 |
EL451713 | 301 | 228 | 527 | 0 |
DY275245 | 312 | 3 | 310 | 0 |
DY275245 | 114 | 264 | 365 | 0.016 |
Sequence Alignments (This image is cropped. Click for full image.) |
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