| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20002967m |
| Family | AA7 |
| Protein Properties | Length: 523 Molecular Weight: 57420.4 Isoelectric Point: 7.7954 |
| Chromosome | Chromosome/Scaffold: 2 Start: 3299616 End: 3303299 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 90 | 270 | 0 |
| DFPGLIVVPGSEADLRSALYFASKTRIRVVVRCSGHDFNGRSSGRGVMLIKTERLNWTSYDASSQTISFGAGANHEIVYTALVPHNRMYVGGQSKTVCPA GCLAGGCHGLLSRQYGLGIDSILEIRFALFNGTIITLNRTRYADLFNAYLGAGQNSFGIAVSFKAQTYPAPPVIIMLDAEF | |||
| Full Sequence |
|---|
| Protein Sequence Length: 523 Download |
| MDSSRGRYFK PTRQCRLCRF ALIFCIAGAL RSADAATGFC ISAPGSCWPS AARIRAWIST 60 LSNSTTVYTP DAEPNIFLSE ATAMNFLKSD FPGLIVVPGS EADLRSALYF ASKTRIRVVV 120 RCSGHDFNGR SSGRGVMLIK TERLNWTSYD ASSQTISFGA GANHEIVYTA LVPHNRMYVG 180 GQSKTVCPAG CLAGGCHGLL SRQYGLGIDS ILEIRFALFN GTIITLNRTR YADLFNAYLG 240 AGQNSFGIAV SFKAQTYPAP PVIIMLDAEF VINSPFVTSG NLLTNFFLNT TWFNEMPRQL 300 SGTINLDSGR ARVKFVYTGT DYDDLSAKLA PLLASPFRSA VAEPQFFSNL AEMALNMYPA 360 ETEIWGRKYI TSGFLPPDQD TLDSVASVIA TTNPYMWLWF VFGGAVPEKA GIGSVPDGMR 420 YAMYEVLFGT HWFNPNDDRL RVESLEPYLP LLYGISPTSY SNEFTSWGSY NDIQDWKTRF 480 FSNYSNLLAV KKKYDPCNLI TATYAVGSDE PVAICSCAPK SA* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 9.0e-5 | 472 | 499 | 29 | + 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-16 | 92 | 227 | 148 | + 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 | 9.0e-19 | 67 | 270 | 214 | + 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 |
| EMBL | CBF81578.1 | 1e-24 | 104 | 510 | 130 | 550 | TPA: FAD/FMN-containing isoamyl alcohol oxidase MreA (AFU_orthologue; AFUA_6G03620) [Aspergillus nidulans FGSC A4] |
| GenBank | EDP47621.1 | 1e-24 | 104 | 510 | 136 | 557 | FAD/FMN-containing isoamyl alcohol oxidase MreA [Aspergillus fumigatus A1163] |
| RefSeq | XP_001265527.1 | 5e-27 | 100 | 509 | 124 | 550 | FAD binding domain protein [Neosartorya fischeri NRRL 181] |
| RefSeq | XP_001394372.1 | 6e-26 | 29 | 509 | 13 | 550 | hypothetical protein An11g03740 [Aspergillus niger] |
| RefSeq | XP_001481692.1 | 1e-24 | 100 | 509 | 124 | 550 | isoamyl alcohol oxidase [Aspergillus fumigatus Af293] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3tsj_B | 0.000000001 | 92 | 337 | 53 | 292 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| PDB | 3tsj_A | 0.000000001 | 92 | 337 | 53 | 292 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| PDB | 3tsh_A | 0.000000001 | 92 | 337 | 53 | 292 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 3rja_A | 0.000000002 | 28 | 263 | 1 | 211 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 3rj8_A | 0.000000002 | 28 | 263 | 1 | 211 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| Signal Peptide | ||||
|---|---|---|---|---|
| Cleavage Site | ||||
| 35 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FD919741 | 234 | 257 | 490 | 0 |
| JK987490 | 179 | 92 | 265 | 0.00000000000004 |
| FC092815 | 223 | 186 | 396 | 0.0000000000002 |
| HO400695 | 172 | 92 | 263 | 0.0000000000003 |
| DW164190 | 208 | 62 | 260 | 0.0000000000003 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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