Basic Information | |
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Species | Linum usitatissimum |
Cazyme ID | Lus10026775 |
Family | AA7 |
Protein Properties | Length: 527 Molecular Weight: 58659.8 Isoelectric Point: 6.5851 |
Chromosome | Chromosome/Scaffold: 361 Start: 520655 End: 523602 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 61 | 523 | 0 |
RFNTTTSFKPSIIVTPDSIPQIQATINCSKTHNLQIRIRSGGHDFEGLSYTSSPQDNSFSSSFLLLDLIRFRNITIHDHNSTAWIQPAVTTGELYYRLHQ VSPTLAFPSGICPTVGLGGHISGGGWGSLLRKYGLAADNVVDAQLIDAKGRFLDRASMGEDLFWAIRGGGGNTFGIVVAWKVKLVTVPVNVTVCNVVKTL EQNATEILHRWQYVVDMQLPDDVFSSVIITSGQASFNTLYLGGTEHLIPIMDNKFPELGLKGENCVETSWARSNLYLLGFPLDTPLETLLDRTTSPIVWG NIKGKSDYVKDPIPINGLEGIWGKLKEVDASTAMLVMESYGGKMKEISESSIPFPHRNGVIYQLQELTFWAEDGQVAADRQINWLRGLYDYMAPYVSKNP REAYVNYRDLDIGTNGGGGGSRWENYLLARSWGLKYYKGNFDRLVGVKTLVDHDNFFRNEQSI |
Full Sequence |
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Protein Sequence Length: 527 Download |
MRRSLNISLL LIVVIFCPYH NLADDQLILD CLYSSNLSQV TYIPTNLTYS SVLQYSIKNG 60 RFNTTTSFKP SIIVTPDSIP QIQATINCSK THNLQIRIRS GGHDFEGLSY TSSPQDNSFS 120 SSFLLLDLIR FRNITIHDHN STAWIQPAVT TGELYYRLHQ VSPTLAFPSG ICPTVGLGGH 180 ISGGGWGSLL RKYGLAADNV VDAQLIDAKG RFLDRASMGE DLFWAIRGGG GNTFGIVVAW 240 KVKLVTVPVN VTVCNVVKTL EQNATEILHR WQYVVDMQLP DDVFSSVIIT SGQASFNTLY 300 LGGTEHLIPI MDNKFPELGL KGENCVETSW ARSNLYLLGF PLDTPLETLL DRTTSPIVWG 360 NIKGKSDYVK DPIPINGLEG IWGKLKEVDA STAMLVMESY GGKMKEISES SIPFPHRNGV 420 IYQLQELTFW AEDGQVAADR QINWLRGLYD YMAPYVSKNP REAYVNYRDL DIGTNGGGGG 480 SRWENYLLAR SWGLKYYKGN FDRLVGVKTL VDHDNFFRNE QSIPPL* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-11 | 70 | 240 | 178 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-15 | 70 | 214 | 146 | + 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. | ||
pfam08031 | BBE | 2.0e-15 | 463 | 524 | 62 | + 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 |
RefSeq | XP_002299020.1 | 0 | 28 | 526 | 31 | 530 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002299022.1 | 0 | 28 | 526 | 24 | 523 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002300557.1 | 0 | 28 | 526 | 31 | 528 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002332196.1 | 0 | 29 | 526 | 25 | 524 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002334045.1 | 0 | 28 | 526 | 31 | 528 | 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 | 28 | 526 | 13 | 496 | 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 | 28 | 526 | 13 | 496 | 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 | 23 | 526 | 6 | 496 | 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 | 23 | 526 | 6 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
PDB | 3tsh_A | 0 | 23 | 526 | 6 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |