| Basic Information | |
|---|---|
| Species | Arabidopsis lyrata |
| Cazyme ID | 354696 |
| Family | AA7 |
| Protein Properties | Length: 548 Molecular Weight: 62293.1 Isoelectric Point: 8.5891 |
| Chromosome | Chromosome/Scaffold: 7 Start: 9567571 End: 9570200 |
| 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 | 92 | 312 | 0 |
| NFTSLKPILIVKPKTESEIKQSILCSRKLGVQVRTMSGGHDYEGLSYLSQSPFIIVDLVNIRSINLNLTDDNAWIQSGATLGELYYKIAKTSKIHAFAAG ICPSVGVGGHISGGGFGTIMRKHGLASDNVVDARLMDVNGKILDRKTMGEDLFWALRGGGAASFGVVLSWKVKLARVPEKVTCFISQHTMGPSMNKLVHR WQSIGSELDEDLFIRVIIDNS | |||
| Full Sequence |
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| Protein Sequence Length: 548 Download |
| MELINITIGY KTEQCDFASD EASFQHNADE FQCVKSVYST PTREQFQNCL STKQFNSTFQ 60 NPINLTTHKP DSRVYTDFSE SSSPNSSFLN LNFTSLKPIL IVKPKTESEI KQSILCSRKL 120 GVQVRTMSGG HDYEGLSYLS QSPFIIVDLV NIRSINLNLT DDNAWIQSGA TLGELYYKIA 180 KTSKIHAFAA GICPSVGVGG HISGGGFGTI MRKHGLASDN VVDARLMDVN GKILDRKTMG 240 EDLFWALRGG GAASFGVVLS WKVKLARVPE KVTCFISQHT MGPSMNKLVH RWQSIGSELD 300 EDLFIRVIID NSLEGNQRRV KSTFQTLFLG GIDRLIPLMN QKFPELGLRS QDCSEMSWIE 360 SIMFFNWRSG QPLEILLNRD LRFEDQYFKA KSDYVQKPVP ENVFEEVTKR FLEQDTPLMI 420 FEPLGGKISK IPETESPYPH RRGNLYNIQY MVKWKVNEVE EMNKHVRWVR SLHDYMTPYV 480 SKSPRGAYLN YRDLDLGSTK GINTSFEDAR KWGETYFKGN FKRLGLVKGK IDPTNFFRNE 540 QSIPPLF* 600 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 1.0e-9 | 98 | 546 | 477 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 3.0e-15 | 98 | 235 | 142 | + 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 | 2.0e-17 | 487 | 544 | 58 | + 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 | AAK56258.1 | 0 | 33 | 547 | 16 | 530 | AF367269_1 AT4g20860/T13K14_20 [Arabidopsis thaliana] |
| GenBank | AAN60251.1 | 0 | 33 | 470 | 14 | 451 | unknown [Arabidopsis thaliana] |
| RefSeq | NP_193818.1 | 0 | 33 | 547 | 16 | 530 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | NP_199249.1 | 0 | 43 | 546 | 30 | 530 | FAD-binding domain-containing protein [Arabidopsis thaliana] |
| RefSeq | XP_002523167.1 | 0 | 39 | 544 | 19 | 522 | 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 | 43 | 546 | 4 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_B | 0 | 95 | 547 | 50 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsj_A | 0 | 95 | 547 | 50 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 3tsh_A | 0 | 95 | 547 | 50 | 497 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
| PDB | 4dns_B | 0 | 65 | 547 | 17 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| Hydropathy |
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| EST Download unfiltered results here | ||||
|---|---|---|---|---|
| Hit | Length | Start | End | EValue |
| EX137437 | 303 | 102 | 404 | 0 |
| BX835362 | 261 | 283 | 543 | 0 |
| GT085426 | 306 | 209 | 513 | 0 |
| ES911178 | 232 | 317 | 548 | 0 |
| BE662929 | 217 | 209 | 425 | 0 |
| Sequence Alignments (This image is cropped. Click for full image.) |
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