Basic Information | |
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Species | Phaseolus vulgaris |
Cazyme ID | Phvul.006G125000.1 |
Family | AA7 |
Protein Properties | Length: 561 Molecular Weight: 63043.8 Isoelectric Point: 9.198 |
Chromosome | Chromosome/Scaffold: 06 Start: 23982130 End: 23984092 |
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 | 68 | 526 | 0 |
NLRFNTSTTPKPFLIVTPFHVSHVQTAVVCAKRHNLLMKIRSGGHDYEGVSYVASHPFFLLDMFNLRSIDFDMESEVAWVQAGATLGEVYYRIAEKSKTH GFPAGVCPTVGVGGHISGGGYGNLMRKYGTAVDNVVDAQIVDAQGRLLNRRSMGEDLFWAVRGGGGGSFGVIIAYKIKLVRVPEKVTVFKVGKTLEQNAT NIVYNWQHVAPTIDNNLFIRLILEVVNGTEVGTKTVRATFIALFLGDSKSLVSLMKDKFPELGLKQSDCIETSWLQSVMFWDNIDIATPVEILLERQPQS LKYLKRKSDYVKKPISKEGWEGIWKKMIELEKAVMFLNPYGGRMGEIPSTETPLPHRAGNLWKIQYQGNWYEAGEEVAQYHINLLRELYKYMTPFVSQNP RQAFMCYKDLDLGINHHGFLGYFEGSAYGVQYFNDNFKRLVEIKSKVDPTNFFRTEQSI |
Full Sequence |
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Protein Sequence Length: 561 Download |
MGLLSSRTLF SIVSLLCLLC SYFAPNSAHN TFVHCLLNHS EPSYPISAAI FSQNSSSFSS 60 VLQAYIRNLR FNTSTTPKPF LIVTPFHVSH VQTAVVCAKR HNLLMKIRSG GHDYEGVSYV 120 ASHPFFLLDM FNLRSIDFDM ESEVAWVQAG ATLGEVYYRI AEKSKTHGFP AGVCPTVGVG 180 GHISGGGYGN LMRKYGTAVD NVVDAQIVDA QGRLLNRRSM GEDLFWAVRG GGGGSFGVII 240 AYKIKLVRVP EKVTVFKVGK TLEQNATNIV YNWQHVAPTI DNNLFIRLIL EVVNGTEVGT 300 KTVRATFIAL FLGDSKSLVS LMKDKFPELG LKQSDCIETS WLQSVMFWDN IDIATPVEIL 360 LERQPQSLKY LKRKSDYVKK PISKEGWEGI WKKMIELEKA VMFLNPYGGR MGEIPSTETP 420 LPHRAGNLWK IQYQGNWYEA GEEVAQYHIN LLRELYKYMT PFVSQNPRQA FMCYKDLDLG 480 INHHGFLGYF EGSAYGVQYF NDNFKRLVEI KSKVDPTNFF RTEQSIPVLT LVEFGKLITG 540 KSVLSVLFGL FAIHWIRNLK * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 1.0e-12 | 470 | 527 | 58 | + 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-14 | 61 | 529 | 498 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 1.0e-18 | 79 | 216 | 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 |
EMBL | CAN60572.1 | 0 | 24 | 529 | 24 | 529 | hypothetical protein [Vitis vinifera] |
EMBL | CAN80091.1 | 0 | 24 | 529 | 24 | 529 | hypothetical protein [Vitis vinifera] |
RefSeq | XP_002269462.1 | 0 | 24 | 529 | 24 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002270585.1 | 0 | 24 | 529 | 24 | 529 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002523152.1 | 0 | 24 | 529 | 4 | 508 | Reticuline oxidase precursor, 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 | 4dns_B | 0 | 32 | 529 | 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 | 32 | 529 | 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 | 22 | 529 | 1 | 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 | 22 | 529 | 1 | 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 | 22 | 529 | 1 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |