| Basic Information | |
|---|---|
| Species | Volvox carteri |
| Cazyme ID | Vocar20002817m |
| Family | AA7 |
| Protein Properties | Length: 514 Molecular Weight: 56544 Isoelectric Point: 6.8818 |
| Chromosome | Chromosome/Scaffold: 2 Start: 3296645 End: 3298186 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 79 | 282 | 0 |
| NALKTNFPGIIVAPVSENDLSSSLQFAYNYKIRVVTRCSGQDYNGRSNGRGVMMIRMEKFNYVEYNPDDETVTFGAGATQEMVYAVVADVNRVFVGGLST SICPAGCLAGGCYGPLSRLRGLGIDNILQIRFMLYNGTILTLSRTRYADLFHAYLGAGQNSFGVAISFTARTFPAPRQILQLEVQLDLINPALGGATYPN LFSD | |||
| Full Sequence |
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| Protein Sequence Length: 514 Download |
| MVAPQVSPQH GPLAILVIAA SITMLAGTGH GAFCQPNSGT CWPDRAALST WISRLSGATN 60 VYQWDRTPDK FLSAAATANA LKTNFPGIIV APVSENDLSS SLQFAYNYKI RVVTRCSGQD 120 YNGRSNGRGV MMIRMEKFNY VEYNPDDETV TFGAGATQEM VYAVVADVNR VFVGGLSTSI 180 CPAGCLAGGC YGPLSRLRGL GIDNILQIRF MLYNGTILTL SRTRYADLFH AYLGAGQNSF 240 GVAISFTART FPAPRQILQL EVQLDLINPA LGGATYPNLF SDYIFNVRWF NSLPNELSGT 300 ILVSGNSVHI RFFYAGEDYV GAFNSLQPML NSPYRTSVTP ITNYSSILEM VRETQPASAE 360 IWSRTFIANT FVAPRQDILN NASRIIGESQ PSMWLWFMFG GAVQASSTGS VPAGMRGAMY 420 EVLFADKWFD PAEDEPRMDY INSAYLPTLY AFGSSSYNNE YTTWGNRFNT LNDWKSRFFN 480 DYNRLVGVKS KYDPCNLFTV RFGVASDLPT ATC* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam08031 | BBE | 0.0001 | 467 | 504 | 39 | + 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 | 7.0e-20 | 86 | 221 | 140 | + 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 | 4.0e-21 | 52 | 271 | 229 | + 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 |
| RefSeq | XP_002523162.1 | 3e-24 | 86 | 498 | 80 | 522 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002523164.1 | 7e-24 | 86 | 498 | 80 | 522 | Reticuline oxidase precursor, putative [Ricinus communis] |
| RefSeq | XP_002569125.1 | 2e-23 | 85 | 507 | 124 | 589 | Pc21g21500 [Penicillium chrysogenum Wisconsin 54-1255] |
| RefSeq | YP_001644506.1 | 2e-23 | 66 | 506 | 16 | 449 | FAD linked oxidase domain-containing protein [Bacillus weihenstephanensis KBAB4] |
| RefSeq | ZP_04261492.1 | 2e-23 | 66 | 506 | 16 | 449 | FAD linked oxidase domain protein [Bacillus cereus BDRD-ST196] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3rja_A | 0.000000005 | 86 | 347 | 37 | 296 | A Chain A, H71s Mutant Of The Antibiotic Resistance Protein Nima From Deinococcus Radiodurans |
| PDB | 3rj8_A | 0.000000005 | 86 | 347 | 37 | 296 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| PDB | 2bvh_D | 0.00000002 | 86 | 258 | 39 | 210 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| PDB | 2bvh_C | 0.00000002 | 86 | 258 | 39 | 210 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| PDB | 2bvh_B | 0.00000002 | 86 | 258 | 39 | 210 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
| Signal Peptide | ||||
|---|---|---|---|---|
| Cleavage Site | ||||
| 31 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| FD919741 | 239 | 251 | 488 | 0 |
| FC092815 | 120 | 180 | 298 | 6e-22 |
| JK514446 | 185 | 79 | 257 | 2e-16 |
| EL421203 | 181 | 86 | 262 | 5e-16 |
| DY908315 | 185 | 86 | 266 | 5e-16 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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