| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma09g03090.1 |
| Family | AA7 |
| Protein Properties | Length: 544 Molecular Weight: 61209.1 Isoelectric Point: 7.0557 |
| Chromosome | Chromosome/Scaffold: 09 Start: 2178668 End: 2180818 |
| 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 | 295 | 0 |
| APKPELIFTPLTDSHVQVAVTCSKKLGIHLRIRSGGHDYEGLSYVSEVESPFIIVDLSKLRAIDVDIEDNTAWIQAGATIGEVYYRIYEKSSVHGFPAGL CTSLGVGGHITGGAYGSMMRKYGLGADNVVDARIVDANGQILDREAMGEDLFWAIRGGGGASFGILLWWKIKLVPVPETVTVFTVTRSLEQDATKILHRW QEVAPYIDEDLFIRVIIQPATVG | |||
| Full Sequence |
|---|
| Protein Sequence Length: 544 Download |
| MVSPISHLVT LILLLSVSLA ASASLEENFV QCLSFYSDKA APFYASIYTP QNASFNKILE 60 SSAQNLRYLV PSAPKPELIF TPLTDSHVQV AVTCSKKLGI HLRIRSGGHD YEGLSYVSEV 120 ESPFIIVDLS KLRAIDVDIE DNTAWIQAGA TIGEVYYRIY EKSSVHGFPA GLCTSLGVGG 180 HITGGAYGSM MRKYGLGADN VVDARIVDAN GQILDREAMG EDLFWAIRGG GGASFGILLW 240 WKIKLVPVPE TVTVFTVTRS LEQDATKILH RWQEVAPYID EDLFIRVIIQ PATVGNKTER 300 TITTSYNAQF LGGADRLLQV MKESFPELGL TKKDCLETSW IKSVLYIAGY PNDTPPEVLL 360 QGKSTFKNYF KAKSDFVRDP IPETGLEGLW QRLLEEDSPL MIWNPYGGMM SKFSESDIPF 420 PHRNGTLYKI QYLTLWQDGD KNASKHEDWI RKLYNYMTPY VSKFPREAYV NYRDLDLGMN 480 KKNSTSYIQA TAWGNMYFKD NFNRLVKIKT KVDPDNVFRH EQSIPPLPVS SMRLKDKKCK 540 TWE* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR01679 | bact_FAD_ox | 0.004 | 76 | 238 | 166 | + 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. | ||
| TIGR00387 | glcD | 0.0005 | 113 | 214 | 103 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
| pfam08031 | BBE | 4.0e-19 | 468 | 525 | 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 | 1.0e-26 | 76 | 527 | 474 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 4.0e-29 | 76 | 215 | 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 | |
|---|---|
| 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 |
| EMBL | CAN81654.1 | 0 | 11 | 528 | 12 | 528 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002268361.1 | 0 | 11 | 528 | 12 | 528 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299030.1 | 0 | 22 | 528 | 1 | 507 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523162.1 | 0 | 27 | 530 | 31 | 534 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 0 | 19 | 530 | 23 | 534 | 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 | 23 | 528 | 1 | 514 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 22 | 527 | 6 | 496 | 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 | 22 | 527 | 6 | 496 | 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 | 24 | 527 | 6 | 496 | 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 | 24 | 527 | 6 | 496 | 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 |
