| Basic Information | |
|---|---|
| Species | Thellungiella halophila |
| Cazyme ID | Thhalv10007327m |
| Family | AA7 |
| Protein Properties | Length: 535 Molecular Weight: 60008.8 Isoelectric Point: 6.9141 |
| Chromosome | Chromosome/Scaffold: 5 Start: 4092684 End: 4095131 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 73 | 306 | 0 |
| NLRYLMPSNPKPEFIFEPLYETHVQAAVFCAKKLRLHLRLRSGGHDYEGLSYVSEMETAFVIVDLSKLRHINVDLESNTAWVHAGASIGEVYYRIQEKSK IHGFPAGLCTSLGIGGHIIGGAYGSMMRKFGLGADNVLDARIVNADGKILNRAAMGEDVFWAIRGGGGGSFGVILAWKIKLVPVPEIVTVFTVTRTLEQD GTKVLHTWQQVADKLDDDLFIRVIIQPASKTAKS | |||
| Full Sequence |
|---|
| Protein Sequence Length: 535 Download |
| MVFTIIPNAN AFLVTLLLLA LSSIPLSSST IQQDFVMCLV DNSDASFPMD SSFFTNDLNA 60 SSFKLALETS AQNLRYLMPS NPKPEFIFEP LYETHVQAAV FCAKKLRLHL RLRSGGHDYE 120 GLSYVSEMET AFVIVDLSKL RHINVDLESN TAWVHAGASI GEVYYRIQEK SKIHGFPAGL 180 CTSLGIGGHI IGGAYGSMMR KFGLGADNVL DARIVNADGK ILNRAAMGED VFWAIRGGGG 240 GSFGVILAWK IKLVPVPEIV TVFTVTRTLE QDGTKVLHTW QQVADKLDDD LFIRVIIQPA 300 SKTAKSKERT ISTSYQGQFL GDANRLLQVM QRSFPQLGLT KKDCLETSWI KSVMYIAGYP 360 STAPSEALLD GKSLFKNYFK AKSDYVEEPI PIEGLEGLWK KLLEEDSPLT IWNPYGGMMA 420 RIPETETPFP HRSGTLFKIQ WLTLWQDGKA SEAKHMEWMR EMYSYMEQYV SKNPRSAYVN 480 YRDLDLGTNG KGSDAREWGN KYFKGNFERL VKVKAKFDPE NFFRHEQSIP TELE* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 2.0e-18 | 96 | 532 | 456 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 1.0e-18 | 84 | 223 | 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 | 7.0e-21 | 477 | 530 | 54 | + 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 |
| GenBank | AAD25763.1 | 0 | 1 | 431 | 1 | 431 | AC007060_21 Strong similarity to F19I3.2 gi |
| RefSeq | NP_174363.1 | 0 | 1 | 534 | 1 | 534 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_181025.1 | 0 | 1 | 533 | 1 | 531 | MEE23 (MATERNAL EFFECT EMBRYO ARREST 23); FAD binding / catalytic/ electron carrier/ oxidoreductase [Arabidopsis thaliana] |
| RefSeq | XP_002523162.1 | 0 | 28 | 530 | 26 | 529 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 0 | 31 | 530 | 29 | 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 | 67 | 530 | 37 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 25 | 533 | 3 | 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 | 25 | 533 | 3 | 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 | 32 | 530 | 8 | 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 | 32 | 530 | 8 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
