| Basic Information | |
|---|---|
| Species | Chlamydomonas reinhardtii |
| Cazyme ID | g9859.t1 |
| Family | AA7 |
| Protein Properties | Length: 594 Molecular Weight: 59495.2 Isoelectric Point: 5.6791 |
| Chromosome | Chromosome/Scaffold: 9 Start: 4757501 End: 4762082 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 51 | 178 | 4.1e-39 |
| RPLLCFRPESKHDVLHACAVAATHGLKVSPRGSGHHYGGCSLVSGCLLLDLSALNSVTVDVAARTAAVGPCVSGRELRAATAPAGLHFPGPHLSEVGLSG FILGGGNGWGVRHWGAAADNVIEFEAVV | |||
| Full Sequence |
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| Protein Sequence Length: 594 Download |
| MPQTPQADAA TICEELFAVT GLRAEVVDGS WNLPSWNGLL NGESPVIKPP RPLLCFRPES 60 KHDVLHACAV AATHGLKVSP RGSGHHYGGC SLVSGCLLLD LSALNSVTVD VAARTAAVGP 120 CVSGRELRAA TAPAGLHFPG PHLSEVGLSG FILGGGNGWG VRHWGAAADN VIEFEAVVFG 180 HTPAAGPAPA GADGNGSSSS NGNGDGSSSS SAYGAGSSSS NGNGDGSSSS SAYGAGGPRL 240 VRVTAESDPE LFWGLKGAGS FLAVVTGFVL RLHPVPPALP LTCAIYPLTA LEQVAAFFQR 300 FHTSLPSYIE GSLAIVGGGD GGGSEDDGAD GGGSSGSSEG VGSSGAAGRR RVTPVVIVSC 360 TAFVEAGRPE VEAAYAQLRG FLPDTRISIQ EGPLPYDAAL SILDPGWSWP GLCMYGHGCF 420 VPVPALVVQA AAEGEASAGC GGALAALRQA ADTMTSPRSI LLVCPSAPST APGCSSSSSS 480 SSSSSSSSSS GDGSSGSSCS GAFGFRDTFY TAAYAMWTRT PQGPAADGDA AHAAWVRAAA 540 AGLSPHVSGL YVNEVMHDQP GNSQVRGSYE AAAYVRLRAL KARLDPGGLL RAL* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 0.006 | 47 | 144 | 99 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 0.002 | 52 | 89 | 38 | + 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. | ||
| Annotations - NR Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| RefSeq | YP_001108190.1 | 8e-38 | 36 | 590 | 30 | 449 | FAD linked oxidase-like [Saccharopolyspora erythraea NRRL 2338] |
| RefSeq | YP_003394206.1 | 1e-23 | 51 | 591 | 49 | 461 | FAD linked oxidase domain protein [Conexibacter woesei DSM 14684] |
| RefSeq | YP_356778.1 | 1e-18 | 36 | 306 | 46 | 251 | FAD/FMN-containing dehydrogenase [Pelobacter carbinolicus DSM 2380] |
| RefSeq | YP_672916.1 | 2e-23 | 48 | 310 | 35 | 241 | FAD linked oxidase-like [Mesorhizobium sp. BNC1] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2bvh_D | 0.00000001 | 51 | 172 | 38 | 159 | A Chain A, Crystal Structure Of Botulinum Neurotoxin Type D Light Chain |
| PDB | 2bvh_C | 0.00000001 | 51 | 172 | 38 | 159 | A Chain A, Crystal Structure Of Botulinum Neurotoxin Type D Light Chain |
| PDB | 2bvh_B | 0.00000001 | 51 | 172 | 38 | 159 | A Chain A, Crystal Structure Of Botulinum Neurotoxin Type D Light Chain |
| PDB | 2bvh_A | 0.00000001 | 51 | 172 | 38 | 159 | A Chain A, Crystal Structure Of Botulinum Neurotoxin Type D Light Chain |
| PDB | 2bvg_D | 0.00000001 | 51 | 172 | 38 | 159 | A Chain A, Crystal Structure Of Botulinum Neurotoxin Type D Light Chain |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| HS283717 | 95 | 502 | 593 | 0.000003 |
| HO889739 | 95 | 502 | 593 | 0.000003 |
| JZ023661 | 64 | 239 | 302 | 0.001 |
| HO480304 | 73 | 240 | 310 | 0.015 |
| GW220347 | 52 | 542 | 593 | 0.14 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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