Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00028562m |
Family | AA7 |
Protein Properties | Length: 532 Molecular Weight: 58209.2 Isoelectric Point: 9.4682 |
Chromosome | Chromosome/Scaffold: 029865 Start: 2182 End: 3777 |
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 | 85 | 317 | 0 |
TVKPLYIVTPTEPCHIQATVSCGRRHGMRLRVRSGGHDYEGLSYRSDKAEPFAVVDLSKMRKVRIDGKQATAWVDSGAQLGEIYYAVAKETPKLGFPAGV CATIGVGGHFSGGGFGMMLRKYGTAADLVVDAKVVDAEGRLLDRKAMGEDLFWAIRGGGGASFGIVVSWQVKLVPVPPTVTVFQIHRGVKDGAVDLVAKW QQVAPSLPEDLMIRILAMGQDALFEALFLGTCK |
Full Sequence |
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Protein Sequence Length: 532 Download |
MQPTTMATSS PRASALALLL CACLSASSFH VAISGPPAPG GGKDDFLSCL TKAVPPRLLF 60 AKSSPAYGSV WSSTVRNIKF LSDKTVKPLY IVTPTEPCHI QATVSCGRRH GMRLRVRSGG 120 HDYEGLSYRS DKAEPFAVVD LSKMRKVRID GKQATAWVDS GAQLGEIYYA VAKETPKLGF 180 PAGVCATIGV GGHFSGGGFG MMLRKYGTAA DLVVDAKVVD AEGRLLDRKA MGEDLFWAIR 240 GGGGASFGIV VSWQVKLVPV PPTVTVFQIH RGVKDGAVDL VAKWQQVAPS LPEDLMIRIL 300 AMGQDALFEA LFLGTCKDLL PLMNARFPEL GMKQADCNEM SWIQSVPFIP LGKSATVKDL 360 LNRTSNIRAF GKYKSDYVRD PIPRGVWEKI FGWLAKPGAG VMIMDPYGGR ISAIDDDATP 420 FPHRQGMLFN IQYVNYWFGE GAGAQPNQWS RDMYAFMEPY VTKNPRQAYV NYRDMDLGVN 480 QVVGDVSTYE SGKVWGEKYF KGNFERLART KAKVDPTDFF RNEQSIPPLL K* 540 |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
COG0277 | GlcD | 2.0e-10 | 82 | 529 | 468 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
pfam01565 | FAD_binding_4 | 2.0e-15 | 88 | 227 | 141 | + 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 | 1.0e-18 | 468 | 527 | 60 | + 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 |
GenBank | AAS02108.1 | 0 | 12 | 530 | 5 | 522 | FAD-linked oxidoreductase BG60 [Cynodon dactylon] |
EMBL | CAH92630.1 | 0 | 12 | 530 | 3 | 518 | pollen allergen Sec c 4 [Secale cereale] |
EMBL | CAH92635.1 | 0 | 10 | 530 | 1 | 516 | pollen allergen Hor v 4 [Hordeum vulgare] |
RefSeq | NP_001148634.1 | 0 | 30 | 531 | 21 | 526 | reticuline oxidase [Zea mays] |
RefSeq | XP_002438540.1 | 0 | 43 | 531 | 38 | 526 | hypothetical protein SORBIDRAFT_10g021680 [Sorghum bicolor] |
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 | 36 | 530 | 3 | 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 | 36 | 530 | 3 | 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 | 39 | 531 | 4 | 498 | 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 | 39 | 531 | 4 | 498 | 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 | 39 | 531 | 4 | 498 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
cannabinoid biosynthesis | RXN-7854 | EC-1.21.3 | tetrahydrocannabinolic acid synthase |