Basic Information | |
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Species | Medicago truncatula |
Cazyme ID | AC233657_27.1 |
Family | AA7 |
Protein Properties | Length: 542 Molecular Weight: 61162.7 Isoelectric Point: 9.5626 |
Chromosome | Chromosome/Scaffold: 2336571 Start: 119988 End: 121613 |
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 | |||
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Family | Start | End | Evalue |
AA7 | 63 | 287 | 0 |
NKRFKTATTPKPLAIITVKDDSHVQETVKCAKSNNIQIRIRSGGHDYEGCSYVSDVPFVILDMFHLNSVDVNLQESTAWVESGATLGKIYYTIAKKSNKL AFPSGVCFTVGAGGHFSGGGYGNLMRKFGLSIDNIIDAKIVDVKGNILDRKSMGEDLFWAIRGGGGASFGVILSWKLQLVPVTPQVIVFDVKRYVSEGAT DIVYKWQLIAPKLHKDLFIRVQPNV |
Full Sequence |
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Protein Sequence Length: 542 Download |
MDTIWKLCFL MATLTIVLSN STTTTKSPIQ HFINCLSHSL VSEVTYTPNN TSFSTILNIK 60 IQNKRFKTAT TPKPLAIITV KDDSHVQETV KCAKSNNIQI RIRSGGHDYE GCSYVSDVPF 120 VILDMFHLNS VDVNLQESTA WVESGATLGK IYYTIAKKSN KLAFPSGVCF TVGAGGHFSG 180 GGYGNLMRKF GLSIDNIIDA KIVDVKGNIL DRKSMGEDLF WAIRGGGGAS FGVILSWKLQ 240 LVPVTPQVIV FDVKRYVSEG ATDIVYKWQL IAPKLHKDLF IRVQPNVVQI GQEGKKVVQV 300 SFIGQFLGKI ERLLVLLSKK FPELGLNKSD CFSMPWINST LFWHDKPIGT PLEALLDEPK 360 DPQPLYKKYK SDYVKKPIPK EAIESIWKLM IEGEDLFMQW NPYGGRMKEI LPSETPFPHR 420 AGNLFLILYI NIWSNESSEV SERHMNFSRS FYEFMTPYVS NSPREAFLNY RDADIGANHP 480 SNVTRFGIAK TYGSKFFKGN FERLVSVKTK VDPENFFRYE QSIPTKIIVK VILNDQNKSH 540 M* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam08031 | BBE | 2.0e-15 | 466 | 524 | 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 | 1.0e-16 | 74 | 526 | 475 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam01565 | FAD_binding_4 | 9.0e-23 | 74 | 211 | 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 | |
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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 |
GenBank | ABD32596.1 | 0 | 1 | 524 | 1 | 538 | FAD linked oxidase, N-terminal; TonB box, N-terminal [Medicago truncatula] |
GenBank | ABD32598.1 | 0 | 118 | 527 | 1 | 392 | FAD linked oxidase, N-terminal [Medicago truncatula] |
GenBank | ABD32602.1 | 0 | 1 | 527 | 14 | 542 | FAD linked oxidase, N-terminal [Medicago truncatula] |
GenBank | ABD32603.1 | 0 | 1 | 526 | 1 | 526 | FAD linked oxidase, N-terminal [Medicago truncatula] |
RefSeq | XP_002299010.1 | 0 | 14 | 524 | 3 | 515 | predicted protein [Populus trichocarpa] |
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 | 4dns_B | 0 | 30 | 524 | 11 | 494 | 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 | 30 | 524 | 11 | 494 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3vte_A | 0 | 27 | 524 | 2 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 30 | 527 | 9 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 30 | 527 | 9 | 497 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |