| Basic Information | |
|---|---|
| Species | Medicago truncatula |
| Cazyme ID | Medtr4g091190.1 |
| Family | AA7 |
| Protein Properties | Length: 535 Molecular Weight: 60369.3 Isoelectric Point: 9.0316 |
| Chromosome | Chromosome/Scaffold: 4 Start: 31176489 End: 31178093 |
| 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 | 67 | 288 | 0 |
| NKRFKTATSPKALAIITPKDDSHVQTTIKCAKINNFQLRIRSGGHDYEGFSYLSDVPYVIIDLLHLNSVEVNLQDETTWVEAGATLGKIYYTISKKNNSL AFPSGVCFSLGAGGHFSGGGYGNLMRKFGLSIDNIIDAKIVDVNGNILDRKSMGEDLFWAIRGGGGASFGVILSWKLKLVQVTPQVTVFNVKRNMDEGAT DVVYKWQLVAPKLHKDIFIRAQ | |||
| Full Sequence |
|---|
| Protein Sequence Length: 535 Download |
| METMRALFFL LTTLTIFMSV STTTSLSPIQ NLLNCFYHYS QSFNSSDIIY GPKNPSFSTI 60 LNMKIHNKRF KTATSPKALA IITPKDDSHV QTTIKCAKIN NFQLRIRSGG HDYEGFSYLS 120 DVPYVIIDLL HLNSVEVNLQ DETTWVEAGA TLGKIYYTIS KKNNSLAFPS GVCFSLGAGG 180 HFSGGGYGNL MRKFGLSIDN IIDAKIVDVN GNILDRKSMG EDLFWAIRGG GGASFGVILS 240 WKLKLVQVTP QVTVFNVKRN MDEGATDVVY KWQLVAPKLH KDIFIRAQHN VVTISGKKIV 300 QVSFIGQFLG TIERLLPLIN ESFPELGLKK NDCSSMPWIN STFFWYDIPI GTPLEALLDE 360 PKDPKPIYIK GQSDYVKKPI PKKDIESIWK LMVEGETLSM QWNPYGGRME EILPSETPFP 420 HRAGNLFLIQ YINSWIEESP GAIEHRVNFS RLFHEFMTPY VSNSPREAFL NYRDADVGAN 480 HPSNATKIDV ARTYGSKYFK ENFERLVSVK TKVDPENFFR YEQSIPSRLS KTHI* 540 |
| Functional Domains Download unfiltered results here | ||||||
|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
| pfam08031 | BBE | 3.0e-15 | 468 | 526 | 59 | + 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 | 2.0e-15 | 78 | 520 | 463 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
| pfam01565 | FAD_binding_4 | 1.0e-20 | 78 | 215 | 139 | + 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 |
| GenBank | ABD32596.1 | 0 | 1 | 526 | 1 | 538 | FAD linked oxidase, N-terminal; TonB box, N-terminal [Medicago truncatula] |
| GenBank | ABD32598.1 | 0 | 122 | 534 | 1 | 397 | FAD linked oxidase, N-terminal [Medicago truncatula] |
| GenBank | ABD32602.1 | 0 | 1 | 534 | 14 | 547 | FAD linked oxidase, N-terminal [Medicago truncatula] |
| GenBank | ABD32603.1 | 0 | 1 | 528 | 1 | 526 | FAD linked oxidase, N-terminal [Medicago truncatula] |
| RefSeq | XP_002523155.1 | 0 | 30 | 529 | 27 | 525 | 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 | 27 | 526 | 2 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
| PDB | 4dns_B | 0 | 49 | 529 | 26 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 4dns_A | 0 | 49 | 529 | 26 | 497 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_B | 0 | 48 | 531 | 23 | 499 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_A | 0 | 48 | 531 | 23 | 499 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
