| Basic Information | |
|---|---|
| Species | Gossypium raimondii |
| Cazyme ID | Gorai.010G142800.1 |
| Family | AA7 |
| Protein Properties | Length: 532 Molecular Weight: 59248.1 Isoelectric Point: 7.3015 |
| Chromosome | Chromosome/Scaffold: 10 Start: 36273182 End: 36274777 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 65 | 304 | 0 |
| NLRYLMPLVPKPEFIFIPVYESHAKSAVICAKRLAIHLRFRSGGHDYEGLSYASEIETPFILIDLNQLRSINVDVDDNSAWVQAGATVGEVYYRISEKSK THGFPAGLCSSLGIGGHITGGAYGSMMRKYGLGADNVLDARIVDVNGEILDRAAMGEDLFWAIRGGGGASFGVILAWKIKLVAVPETVTVFTVPKTLEQG ATKILYRWQQVADKLDDDLFIRVVIQVTKTSLKGKRTVTT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 532 Download |
| MAFSSTMILP LLLVLLSAFS ATSKSVQENF MQCLDANSEH PIPISAFCSQ TNSSFTSVLN 60 STAQNLRYLM PLVPKPEFIF IPVYESHAKS AVICAKRLAI HLRFRSGGHD YEGLSYASEI 120 ETPFILIDLN QLRSINVDVD DNSAWVQAGA TVGEVYYRIS EKSKTHGFPA GLCSSLGIGG 180 HITGGAYGSM MRKYGLGADN VLDARIVDVN GEILDRAAMG EDLFWAIRGG GGASFGVILA 240 WKIKLVAVPE TVTVFTVPKT LEQGATKILY RWQQVADKLD DDLFIRVVIQ VTKTSLKGKR 300 TVTTAYNALY LGDAERLLQV MDQSFPELGL ARKDCIETSW IKSVLYIAGF PSETPPEVLL 360 EGKSLFKNYF KAKSDFVQQP IPETALEKLW EMLLEEESPL MIWNPYGGMM ANISDSAIPF 420 PHRKGNLFKI QYVTSWYEGS KDATRKHMDW IKGLYDYMSA YVPTSPRGAY VNYRDLDLGM 480 NHNNASYTEA SVWGAMYFKG NFRRLVKIKS KVDPGNFFRH EQSIPVVLDR A* 540 |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| TIGR00387 | glcD | 0.003 | 113 | 254 | 153 | + 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]. |
| COG0277 | GlcD | 1.0e-16 | 91 | 272 | 192 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
| pfam01565 | FAD_binding_4 | 5.0e-17 | 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. |
| pfam08031 | BBE | 1.0e-18 | 469 | 525 | 57 | + 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. |
| 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 | 1 | 525 | 1 | 525 | hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002268361.1 | 0 | 1 | 525 | 1 | 525 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299030.1 | 0 | 23 | 525 | 1 | 504 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002523162.1 | 0 | 28 | 525 | 31 | 529 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 0 | 21 | 525 | 24 | 529 | 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 | 27 | 525 | 4 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 23 | 528 | 6 | 497 | 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 | 23 | 528 | 6 | 497 | 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 | 530 | 6 | 499 | 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 | 530 | 6 | 499 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
