| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G124078_T01 |
| Family | AA7 |
| Protein Properties | Length: 611 Molecular Weight: 65224.2 Isoelectric Point: 9.7811 |
| Chromosome | Chromosome/Scaffold: 7 Start: 167392597 End: 167397094 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
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| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
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| Family | Start | End | Evalue |
| AA7 | 238 | 406 | 1.09301e-43 |
| YTVSGGVLDGEVYHAVAHSSPSNRSSLALTAASCSTIGLGGHISGGGFGPVSRKFMLAADNVLDALLVDAVGRVLDRRAMGEDVFWAIRGGGGGSWGVVY AWKLRLVPVPDTVTVFTPRREGSVDAMAGLVYRWQFVGPALPDEFYLSASLTIGSSSSSSQEDRDLRNV | |||
| Full Sequence |
|---|
| Protein Sequence Length: 611 Download |
| MYTNSSPTSL LLGILSILLS THRHVIASQS PRDNGVRARS LSTCLLASGV RNFSMAGSPG 60 YATIFDFSIQ NLRFAAPGFR KPEAVVLPTS RRGLQRAVLC ARSASLAIRV RSGGHSYEGQ 120 SYTVSGGVLD GKAPFVVIDL MNLNKSPRDN GVRARSLSTC LLASGVRNFS MAGSPGYATI 180 FDFSIQNLRF AAPGIRKPEA VVLPTSRRGL QRAVLCARSA SLAIRVRSGG HSYEGQSYTV 240 SGGVLDGEVY HAVAHSSPSN RSSLALTAAS CSTIGLGGHI SGGGFGPVSR KFMLAADNVL 300 DALLVDAVGR VLDRRAMGED VFWAIRGGGG GSWGVVYAWK LRLVPVPDTV TVFTPRREGS 360 VDAMAGLVYR WQFVGPALPD EFYLSASLTI GSSSSSSQED RDLRNVAFTG LVLGPKEMAM 420 SVLNERFPEL GLAEAEVSEM SWVESAARLA GLSSVDELTS RVSKTKYYGK NKSDYVQRPI 480 SRDSLAAILR YLSDGPPAGY VTMDPYGGAM ARLSATATPF PHRAGNLYAL QYGVTWDSDA 540 GEASVNYIDI DLMGFDESLG PVRLASSVSH ARATWGAAYF TVENFDRLVR AKTLPMSFTM 600 PKAYHCISGR * |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 9.0e-5 | 196 | 246 | 51 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| COG0277 | GlcD | 2.0e-5 | 80 | 145 | 66 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 1.0e-7 | 198 | 246 | 49 | + 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. | ||
| pfam01565 | FAD_binding_4 | 2.0e-8 | 82 | 145 | 64 | + 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 | 8e-28 | 38 | 145 | 28 | 139 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
| DDBJ | BAD03275.1 | 0 | 154 | 594 | 28 | 531 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
| DDBJ | BAF23509.2 | 0 | 154 | 594 | 32 | 535 | Os08g0343600 [Oryza sativa Japonica Group] |
| RefSeq | NP_001061595.1 | 4e-28 | 33 | 145 | 31 | 147 | Os08g0343600 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001061595.1 | 0 | 149 | 594 | 31 | 539 | Os08g0343600 [Oryza sativa (japonica cultivar-group)] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 3fw9_A | 0 | 157 | 594 | 2 | 478 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 3fw9_A | 2e-17 | 41 | 149 | 2 | 106 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
| PDB | 4ec3_A | 0 | 155 | 594 | 6 | 484 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 4ec3_A | 1e-17 | 39 | 149 | 6 | 112 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
| PDB | 3gsy_A | 0 | 155 | 594 | 6 | 484 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
