Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G078906_T01 |
Family | AA7 |
Protein Properties | Length: 559 Molecular Weight: 59260.3 Isoelectric Point: 8.74 |
Chromosome | Chromosome/Scaffold: 10 Start: 78060284 End: 78062034 |
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 | 62 | 528 | 0 |
AGAPKPAAVVVPASLQELCDAVRCARGAGLALRLRSGGHSYEGQSYTTSDGGGAFAVVDLAALDRVRVDAARRTAWVQAGATLGQAYRAVAAASPALALS AGSCPTVGSGGHIAGGGFGLLSRKHGLAGDNVVDAVLVDARGRVLDRAAMGEDVFWAIRGGGGGAWGAVYAWRVRLSPVPERVTAFVVNRPGPARSVASL VSTWQHVAPWLPDEFYVSAFVGAGLPEADPGRRAAGVSVTFKGLYLGPAHEAMQILAARFPEIGLSDLAPREMSWIESVVFFSGLPEGSAVSDLADRVLH TKTYFKAKSDYVRRPTPLDHLVKAVGLLSEQPKAYVILDPYGGAMDRVGSAVLPFPHRKGNIHGIQYMVEWTAGDDERREEYMGWLRRFYDFMGAYVATE PRAAYVNYMDLDLGTNDWSDADERSPNPQVEAARAWGERYFLGNYDRLVRAKTLIDPDNVFRNAQSI |
Full Sequence |
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Protein Sequence Length: 559 Download |
MAALALLPLV LRLFAVQAGG RVDGRFTACL AAAGVGNVTT RQSPGYAAAL LVSVQNLRFA 60 GAGAPKPAAV VVPASLQELC DAVRCARGAG LALRLRSGGH SYEGQSYTTS DGGGAFAVVD 120 LAALDRVRVD AARRTAWVQA GATLGQAYRA VAAASPALAL SAGSCPTVGS GGHIAGGGFG 180 LLSRKHGLAG DNVVDAVLVD ARGRVLDRAA MGEDVFWAIR GGGGGAWGAV YAWRVRLSPV 240 PERVTAFVVN RPGPARSVAS LVSTWQHVAP WLPDEFYVSA FVGAGLPEAD PGRRAAGVSV 300 TFKGLYLGPA HEAMQILAAR FPEIGLSDLA PREMSWIESV VFFSGLPEGS AVSDLADRVL 360 HTKTYFKAKS DYVRRPTPLD HLVKAVGLLS EQPKAYVILD PYGGAMDRVG SAVLPFPHRK 420 GNIHGIQYMV EWTAGDDERR EEYMGWLRRF YDFMGAYVAT EPRAAYVNYM DLDLGTNDWS 480 DADERSPNPQ VEAARAWGER YFLGNYDRLV RAKTLIDPDN VFRNAQSIPP LGGGAHGMTW 540 STRGISPKAT SNGSTYDI* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam01565 | FAD_binding_4 | 8.0e-5 | 75 | 207 | 133 | + 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 | 5.0e-6 | 135 | 531 | 410 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 3.0e-17 | 465 | 529 | 65 | + 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 | |
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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 | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
DDBJ | BAC65012.1 | 0 | 29 | 557 | 34 | 561 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
GenBank | EAZ05661.1 | 0 | 29 | 557 | 34 | 561 | hypothetical protein OsI_27888 [Oryza sativa Indica Group] |
RefSeq | XP_002264336.1 | 0 | 6 | 531 | 11 | 534 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002445090.1 | 0 | 1 | 557 | 1 | 511 | hypothetical protein SORBIDRAFT_07g003960 [Sorghum bicolor] |
RefSeq | XP_002533924.1 | 0 | 4 | 531 | 9 | 535 | d-lactate dehydrogenase, putative [Ricinus communis] |
Annotations - PDB Download unfiltered results here | |||||||
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Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
PDB | 3fw9_A | 0 | 28 | 531 | 4 | 494 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 3d2j_A | 0 | 28 | 533 | 29 | 521 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 3d2h_A | 0 | 28 | 533 | 29 | 521 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 3d2d_A | 0 | 28 | 533 | 29 | 521 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 4ec3_A | 0 | 28 | 533 | 10 | 502 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |