| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | AC233560_1010.1 |
| Family | AA7 |
| Protein Properties | Length: 577 Molecular Weight: 65572.9 Isoelectric Point: 7.0242 |
| Chromosome | Chromosome/Scaffold: 2335602 Start: 33937 End: 38027 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| Plaza |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA7 | 101 | 204 | 8.5e-30 |
| QNLRFTSNTTAKPLVIVIPLEVPEIQATVICSRRHDMQIRIRSGGHDYEGLSYVSEVPFVVIDLINLREVQVDVEKRSAWVQGGATAGELLYKISQKSKT LGFP | |||
| AA7 | 205 | 310 | 2.4e-30 |
| AADNILDAHIIDVNGRVLDRESMGEDLFWAIRGGGGASFGVIIAWKVKLVHVPSTVTIFRVSRTLEHNATKLIQKWQLVANKLDEDLNIRVILERVNTST QTRKLT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 577 Download |
| MAERGKDKGK AKNKDSFFFQ FATSHTYTQH CHNMLLTSYL TAVAIIALLF SFITSYAADN 60 NHESFIQCLE SYSNHNSTSV SKFVYTQTHS SYSSILRFSV QNLRFTSNTT AKPLVIVIPL 120 EVPEIQATVI CSRRHDMQIR IRSGGHDYEG LSYVSEVPFV VIDLINLREV QVDVEKRSAW 180 VQGGATAGEL LYKISQKSKT LGFPAADNIL DAHIIDVNGR VLDRESMGED LFWAIRGGGG 240 ASFGVIIAWK VKLVHVPSTV TIFRVSRTLE HNATKLIQKW QLVANKLDED LNIRVILERV 300 NTSTQTRKLT IKATFESLFL GGVDGLIPLM EEEFPELGLV REDCTEMSWI ESVIYHGGFT 360 SDFTSDQPLE VLLNRTHSGV LFFKAKSDYV RDPIPDIGLE GLWPMFYEDE AKSAVLIFTP 420 YGGIMDEISE SEIPFPHRAG NIYQIQHLVF WKEEGDKVEK RHINWIRKLY IYMEPFVSKS 480 PRGAYVNYRD LDIGVNNNNG YTSYKKASIW GVKYFKNNFK RLAKVKTKVD PLNFFRSEQS 540 IPSLSRFDNI TIRHNTLPCE EGMQLLEFPD ALHVII* |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 6.0e-12 | 110 | 544 | 481 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 2.0e-13 | 113 | 223 | 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. | ||
| pfam08031 | BBE | 5.0e-18 | 484 | 542 | 59 | + 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 |
| DDBJ | BAB33033.1 | 0 | 36 | 546 | 4 | 534 | CPRD2 [Vigna unguiculata] |
| RefSeq | XP_002277310.1 | 0 | 41 | 547 | 9 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
| RefSeq | XP_002299045.1 | 0 | 45 | 547 | 12 | 533 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002330609.1 | 0 | 60 | 547 | 26 | 534 | predicted protein [Populus trichocarpa] |
| RefSeq | XP_002332196.1 | 0 | 62 | 547 | 21 | 527 | predicted protein [Populus trichocarpa] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3vte_A | 0 | 60 | 544 | 2 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 84 | 544 | 26 | 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 | 84 | 544 | 26 | 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 | 63 | 544 | 9 | 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 | 63 | 544 | 9 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
