| Basic Information | |
|---|---|
| Species | Physcomitrella patens |
| Cazyme ID | Pp1s183_28V6.1 |
| Family | AA7 |
| Protein Properties | Length: 586 Molecular Weight: 63787.5 Isoelectric Point: 8.2575 |
| Chromosome | Chromosome/Scaffold: 183 Start: 274263 End: 276301 |
| 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 | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 124 | 565 | 0 |
| PLYGVQVATTRDVQSAVKFAARHKLRVVVKTSGHDFLGRSSAAGSFLIWMHKWKNITIDESFVSCGGERGNPVVKVDGGVAWGEVYDALKGTGWIVLGGM SLTVSATGGFIQGGGHGALGPSFGLGADNVLQMEVVTADGEFRVVNACHDPELFFSLRGGGGGTFGVVVSVTYKLHKNPSNIVGAFLLLSPSNGTSWSVE TQEEILTVWSRGTVSLDAALWAGYWGFSSVQFVGELVVPATLAAANATLTPIVRALTQIENVTATYYVMRNHSTFQDWHAADYEVIYPGTLTDYTGHRVL LGSRIIPFSALKHPRRLAKSIVAAMALGGNGAVLGHMVIGPGVRAADPHRQTSVTTAWREGIWHLASWSTWEWNATEVTKLAARNNMKGFVKSLHSAFPN AGAYLNEASIDEPQWQRSFWGYSNYRRLMAVKLRVDPLGLFV | |||
| Full Sequence |
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| Protein Sequence Length: 586 Download |
| MLTNRVSIYF VFFLAIGAGV SRGDINLCRC VDSKSACWPS PEDWDAFNVT VCGRLILPKP 60 TGSPCHGPHR SATLCQHIRN NWFDAYLRAD NAGSMQSENW EDDGQKSCSM YAPESSVCHQ 120 GRVPLYGVQV ATTRDVQSAV KFAARHKLRV VVKTSGHDFL GRSSAAGSFL IWMHKWKNIT 180 IDESFVSCGG ERGNPVVKVD GGVAWGEVYD ALKGTGWIVL GGMSLTVSAT GGFIQGGGHG 240 ALGPSFGLGA DNVLQMEVVT ADGEFRVVNA CHDPELFFSL RGGGGGTFGV VVSVTYKLHK 300 NPSNIVGAFL LLSPSNGTSW SVETQEEILT VWSRGTVSLD AALWAGYWGF SSVQFVGELV 360 VPATLAAANA TLTPIVRALT QIENVTATYY VMRNHSTFQD WHAADYEVIY PGTLTDYTGH 420 RVLLGSRIIP FSALKHPRRL AKSIVAAMAL GGNGAVLGHM VIGPGVRAAD PHRQTSVTTA 480 WREGIWHLAS WSTWEWNATE VTKLAARNNM KGFVKSLHSA FPNAGAYLNE ASIDEPQWQR 540 SFWGYSNYRR LMAVKLRVDP LGLFVCRKCV GSELWKEDGN CNRHY* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| TIGR00387 | glcD | 9.0e-5 | 132 | 264 | 136 | + glycolate oxidase, subunit GlcD. This protein, the glycolate oxidase GlcD subunit, is similar in sequence to that of several D-lactate dehydrogenases, including that of E. coli. The glycolate oxidase has been found to have some D-lactate dehydrogenase activity [Energy metabolism, Other]. | ||
| PLN02441 | PLN02441 | 8.0e-7 | 131 | 279 | 162 | + cytokinin dehydrogenase | ||
| pfam08031 | BBE | 1.0e-9 | 526 | 564 | 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. | ||
| COG0277 | GlcD | 3.0e-18 | 122 | 312 | 197 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 6.0e-21 | 124 | 269 | 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. | ||
| 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_001248265.1 | 0 | 29 | 577 | 28 | 566 | hypothetical protein CIMG_02036 [Coccidioides immitis RS] |
| RefSeq | XP_001263995.1 | 0 | 37 | 574 | 35 | 561 | FAD binding domain protein [Neosartorya fischeri NRRL 181] |
| RefSeq | XP_001753121.1 | 0 | 10 | 585 | 2 | 581 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_001774865.1 | 0 | 37 | 575 | 1 | 493 | predicted protein [Physcomitrella patens subsp. patens] |
| RefSeq | XP_753129.2 | 0 | 37 | 574 | 35 | 561 | FAD/FMN-containing protein [Aspergillus fumigatus Af293] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 2bvh_D | 0.00000000000001 | 135 | 315 | 50 | 219 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
| PDB | 2bvh_C | 0.00000000000001 | 135 | 315 | 50 | 219 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
| PDB | 2bvh_B | 0.00000000000001 | 135 | 315 | 50 | 219 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
| PDB | 2bvh_A | 0.00000000000001 | 135 | 315 | 50 | 219 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
| PDB | 2bvg_D | 0.00000000000001 | 135 | 315 | 50 | 219 | A Chain A, Family Gh5 Endo-Beta-Mannanase From Lycopersicon Esculentum (Tomato) |
| Signal Peptide | ||||
|---|---|---|---|---|
| Cleavage Site | ||||
| 23 | ||||
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| DC930835 | 230 | 52 | 281 | 0 |
| DC945352 | 237 | 350 | 586 | 0 |
| DC946499 | 212 | 375 | 586 | 0 |
| DC931996 | 99 | 1 | 99 | 0 |
| EH092233 | 231 | 36 | 264 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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| Phylogeny |
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