Basic Information | |
---|---|
Species | Glycine max |
Cazyme ID | Glyma07g30940.2 |
Family | AA7 |
Protein Properties | Length: 425 Molecular Weight: 47140.6 Isoelectric Point: 6.4632 |
Chromosome | Chromosome/Scaffold: 07 Start: 35916096 End: 35917552 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
---|
NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
---|---|---|---|
Family | Start | End | Evalue |
AA7 | 73 | 288 | 0 |
APKPLAIVTALDESHVQGTVVCAKSNGIQIRIRSGGHDCEGLSYVSDVPFVVLDMFHFGSVDVDIENGTEWVETGATIGEVYYHTAERSGVHAFPGGVCP TVGAGGHFLVVAMEISCVDNIIDARLVDVNGNILDRKSMGEDQFWAIRGGGGGSFGVIHSWKIKFVFVTPKVTVFKVMRNLELEDGAKGLVYKWQLIATK LHEDLFIRVMHDVVDG |
Full Sequence |
---|
Protein Sequence Length: 425 Download |
MSTITPLWFL LTTLTFLLSA TSDSSPLENF LQCLSNHSRP FNIKSHLHPK KSLTFIYIAQ 60 THTHNHRFYA PTAPKPLAIV TALDESHVQG TVVCAKSNGI QIRIRSGGHD CEGLSYVSDV 120 PFVVLDMFHF GSVDVDIENG TEWVETGATI GEVYYHTAER SGVHAFPGGV CPTVGAGGHF 180 LVVAMEISCV DNIIDARLVD VNGNILDRKS MGEDQFWAIR GGGGGSFGVI HSWKIKFVFV 240 TPKVTVFKVM RNLELEDGAK GLVYKWQLIA TKLHEDLFIR VMHDVVDGTQ NANKKTIQVT 300 FIGLFLGQGD QMLSLVNESF PELGLEQKSV RMEWNPYGGK MHEISPSETP FPHRAGNLFL 360 IEYLTSWGQD GVDAGNRYLN ISRSFYEFMT PYVSHSPREA FLNYRDLDIG ANHPSNATNM 420 NIAQ* |
Functional Domains Download unfiltered results here | ||||||||
---|---|---|---|---|---|---|---|---|
Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 6.0e-6 | 76 | 230 | 168 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 4.0e-19 | 76 | 207 | 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 | |
---|---|
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 |
GenBank | ABD32596.1 | 0 | 1 | 334 | 1 | 348 | FAD linked oxidase, N-terminal; TonB box, N-terminal [Medicago truncatula] |
GenBank | ABD32603.1 | 0 | 1 | 424 | 1 | 490 | FAD linked oxidase, N-terminal [Medicago truncatula] |
RefSeq | XP_002299007.1 | 0 | 28 | 424 | 25 | 488 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002317686.1 | 0 | 20 | 424 | 22 | 492 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002529891.1 | 0 | 19 | 424 | 10 | 483 | 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 | 24 | 331 | 1 | 316 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3vte_A | 2e-18 | 336 | 422 | 391 | 478 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 28 | 416 | 9 | 451 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 28 | 416 | 9 | 451 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsh_A | 0 | 28 | 416 | 9 | 451 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Metabolic Pathways | |||
---|---|---|---|
Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |