| Basic Information | |
|---|---|
| Species | Manihot esculenta |
| Cazyme ID | cassava4.1_027438m |
| Family | AA7 |
| Protein Properties | Length: 527 Molecular Weight: 58789.4 Isoelectric Point: 6.8556 |
| Chromosome | Chromosome/Scaffold: 10364 Start: 36213 End: 37793 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 64 | 521 | 0 |
| LRFLTPATPKPLAIIAATDESHVQATVVCAKSSGLQIRVRSGGHDYEGLSYRSEVPFIILDMFNFNKILIQLSNETAWVEAGATLGELYYQIANQSRIHA FPGGVCPTVATGGHFSGGGYGNLMRKFGLSVDNIIDARIVDANGTILDRQSMGEDLFWAIRGGGGASFGVILSWRINLVRVPEIVTIFQIGRTIEQGAAD ILHRWQEVAPYLDKDLFIRATSTIVNSTIKGEKMIEVSFIGLFLGQIDRLLPLINESFPELGLQKIDCEELSWIESTLFFADFPKGTPIDVLLQKPSKPE FYSKGKSDYVKVVIPKSGLETLWKMMLEVGLMFAQFNPYGGRMGEVSETSTPFPHRAGYRFLIQYSTNWQENDGIDTEKQINLLRELYDAMAPYVSKKPR EAFLNYRDDDIGSNPSNFTNFNESKVYGHKYFKNNFIKLTKVKARVDPDNFFKHQQSI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 527 Download |
| MKLSVFFILF ITLVCLAASD DSTLESFLHC LPSHVNSSNP ISKAIIKPSD PSFQSALEAR 60 VKNLRFLTPA TPKPLAIIAA TDESHVQATV VCAKSSGLQI RVRSGGHDYE GLSYRSEVPF 120 IILDMFNFNK ILIQLSNETA WVEAGATLGE LYYQIANQSR IHAFPGGVCP TVATGGHFSG 180 GGYGNLMRKF GLSVDNIIDA RIVDANGTIL DRQSMGEDLF WAIRGGGGAS FGVILSWRIN 240 LVRVPEIVTI FQIGRTIEQG AADILHRWQE VAPYLDKDLF IRATSTIVNS TIKGEKMIEV 300 SFIGLFLGQI DRLLPLINES FPELGLQKID CEELSWIEST LFFADFPKGT PIDVLLQKPS 360 KPEFYSKGKS DYVKVVIPKS GLETLWKMML EVGLMFAQFN PYGGRMGEVS ETSTPFPHRA 420 GYRFLIQYST NWQENDGIDT EKQINLLREL YDAMAPYVSK KPREAFLNYR DDDIGSNPSN 480 FTNFNESKVY GHKYFKNNFI KLTKVKARVD PDNFFKHQQS IPPGFV* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 3.0e-14 | 465 | 522 | 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-23 | 74 | 268 | 203 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-30 | 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. | ||
| Gene Ontology | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | XP_002299007.1 | 0 | 25 | 526 | 25 | 526 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002300550.1 | 0 | 27 | 525 | 1 | 497 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317074.1 | 0 | 14 | 523 | 5 | 514 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523153.1 | 0 | 18 | 507 | 6 | 487 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523154.1 | 0 | 3 | 523 | 10 | 520 | Reticuline oxidase precursor, putative [Ricinus communis] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 25 | 523 | 5 | 512 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 25 | 523 | 11 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 4dns_A | 0 | 25 | 523 | 11 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_B | 0 | 25 | 523 | 9 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_A | 0 | 25 | 523 | 9 | 495 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| Metabolic Pathways | |||
|---|---|---|---|
| Pathway Name | Reaction | EC | Protein Name |
| cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |
