| Basic Information | |
|---|---|
| Species | Glycine max |
| Cazyme ID | Glyma09g03130.1 |
| Family | AA7 |
| Protein Properties | Length: 534 Molecular Weight: 58871.6 Isoelectric Point: 8.9182 |
| Chromosome | Chromosome/Scaffold: 09 Start: 2211580 End: 2213181 |
| 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 | 71 | 338 | 0 |
| NAGFNTSSTTKPLLIVTPMVESHVQAAVLCAKSANVQLRIRSGGHDYEGLSYISPKPFILLDMSNLRTITVDVKNELAVVQAGAILGELYYRIWEKSKVH GFSAAVCPTVGVGGHISGGGYGTMLRKYGLSVDNVIDAQIVDVKGNLLNRKTMGEDLFWAIRGGGGASFGVIVSFTIKIVPVPETVTFFRVDRTLEQNAT DLVLQWQQVAPTTDDRLFMRLLLSPSGKTATASVVALFLGGANELLPILDKQFPLLGLKKENCTEGRW | |||
| Full Sequence |
|---|
| Protein Sequence Length: 534 Download |
| MAKPSLFYLS AAFVFLSVSS SLSARPPNPP IHDTFLQCLT QHANSTTPLA DIVFDNTNPK 60 FPIVLANYIR NAGFNTSSTT KPLLIVTPMV ESHVQAAVLC AKSANVQLRI RSGGHDYEGL 120 SYISPKPFIL LDMSNLRTIT VDVKNELAVV QAGAILGELY YRIWEKSKVH GFSAAVCPTV 180 GVGGHISGGG YGTMLRKYGL SVDNVIDAQI VDVKGNLLNR KTMGEDLFWA IRGGGGASFG 240 VIVSFTIKIV PVPETVTFFR VDRTLEQNAT DLVLQWQQVA PTTDDRLFMR LLLSPSGKTA 300 TASVVALFLG GANELLPILD KQFPLLGLKK ENCTEGRWID SVIWFDDEEA FEKGAKPEVL 360 LERNPNWALF LKRKSDYVQN AIPREGLELL WKTIIEMGKT GLAFNPYGGK MSQILPDATP 420 FPHRKGNLFK IQYSVTWSDP SPAAAQNFLN QTRVLYSVMT PYVSKNPRSA FLNYRDIDIG 480 TNSFGKNSFE EGEVYGAKYF NANFQRLVKV KTAVDPENFF AYEQSIPVSP TKA* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PRK11230 | PRK11230 | 0.0003 | 80 | 256 | 198 | + glycolate oxidase subunit GlcD; Provisional | ||
| TIGR00387 | glcD | 0.0001 | 129 | 256 | 141 | + 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 | 3.0e-14 | 470 | 527 | 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. | ||
| pfam01565 | FAD_binding_4 | 3.0e-20 | 82 | 219 | 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. | ||
| COG0277 | GlcD | 3.0e-22 | 62 | 520 | 479 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| 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_002267223.1 | 0 | 31 | 527 | 34 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002268606.1 | 0 | 31 | 527 | 34 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299028.1 | 0 | 1 | 533 | 1 | 536 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002317087.1 | 0 | 1 | 533 | 1 | 535 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523157.1 | 0 | 31 | 533 | 36 | 539 | 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 | 4dns_B | 0 | 31 | 527 | 9 | 494 | 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 | 31 | 527 | 9 | 494 | 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 | 27 | 527 | 3 | 494 | 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 | 27 | 527 | 3 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsh_A | 0 | 27 | 527 | 3 | 494 | 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 |
