| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G143530_T01 |
| Family | AA7 |
| Protein Properties | Length: 528 Molecular Weight: 56242.9 Isoelectric Point: 9.1148 |
| Chromosome | Chromosome/Scaffold: 7 Start: 167387814 End: 167389578 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
| Family | Start | End | Evalue |
| AA7 | 79 | 326 | 0 |
| IRKPEAVVLPTSRRGLQRAVLCARSASLAIRVRSGGHSYEGQSYTVSGGVLDGKAPFVVIDLMNLNKVRVHAASATAWAESGATLGEVYHAVAHSSPSNR SSLALTAASCSTIGLGGHISGGGFGPVSRKFMLAADNVLDALLVDAVGRVLDRRAMGEDVFWAIRGGGGGSWGVVYAWKLRLVPVPDTVTVFTPRREGSV DAMAGLVYRWQFVGPALPDEFYLSASLTIGSSSSSSQEDRDLRNVAFT | |||
| Full Sequence |
|---|
| Protein Sequence Length: 528 Download |
| MYTNSSPTSL LLGILSILLS THPHVIASQS PRDNGVRARS LSTCLLASGV RNFSMAGSPG 60 YATIFDFSIQ NLRFAAPGIR KPEAVVLPTS RRGLQRAVLC ARSASLAIRV RSGGHSYEGQ 120 SYTVSGGVLD GKAPFVVIDL MNLNKVRVHA ASATAWAESG ATLGEVYHAV AHSSPSNRSS 180 LALTAASCST IGLGGHISGG GFGPVSRKFM LAADNVLDAL LVDAVGRVLD RRAMGEDVFW 240 AIRGGGGGSW GVVYAWKLRL VPVPDTVTVF TPRREGSVDA MAGLVYRWQF VGPALPDEFY 300 LSASLTIGSS SSSSQEDRDL RNVAFTGLVL GPKEMAMSVL NERFPELGLA EAEVSEMSWV 360 ESAARLAGLS SVDELTSRVS KTKYYGKNKS DYVQRPISRD SLAAILRYLS DGPPAGYVTM 420 DPYGGAMARL SATATPFPHR AGNLYALQYG VTWDSDAGEA SVNYIDIDLM GFDESLGPVR 480 LASSVSHARA TWGAAYFTVE NFDRLVRAKT LPMSFTMPKA YHCISGR* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 3.0e-6 | 80 | 149 | 70 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 4.0e-9 | 82 | 147 | 66 | + 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 |
| DDBJ | BAD03275.1 | 0 | 38 | 511 | 28 | 531 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
| DDBJ | BAF23509.2 | 0 | 38 | 511 | 32 | 535 | Os08g0343600 [Oryza sativa Japonica Group] |
| GenBank | EAZ05659.1 | 0 | 14 | 510 | 9 | 511 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
| RefSeq | NP_001061595.1 | 0 | 33 | 511 | 31 | 539 | Os08g0343600 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002445086.1 | 0 | 40 | 511 | 38 | 543 | hypothetical protein SORBIDRAFT_07g003920 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3fw9_A | 0 | 41 | 511 | 2 | 478 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 4ec3_A | 0 | 39 | 511 | 6 | 484 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 39 | 511 | 6 | 484 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2j_A | 0 | 41 | 511 | 27 | 503 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
| PDB | 3d2h_A | 0 | 41 | 511 | 27 | 503 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
