Basic Information | |
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Species | Citrus sinensis |
Cazyme ID | orange1.1g008779m |
Family | AA7 |
Protein Properties | Length: 555 Molecular Weight: 61859.6 Isoelectric Point: 9.4402 |
Chromosome | Chromosome/Scaffold: 00010 Start: 32916 End: 34628 |
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 | 79 | 309 | 0 |
QNLRFSTPNTPKPQVIITPLDVSQVQAAIKCSKKHGFQIRVRSGGHDFEGLSYVSQVPFVVIDLINLSKISVDAKQKTAWVQSGATLGQLYYRIADKSKN LGFPGGVCPTVGVGGHFSGGGYGIMLRKFGLAADNIVDAHLIDARGRLLDRKSMGQDLFWAIRGGGGTSFGVVVAWKLRLVTVPSTVTRFRITRTLEQNA TKIVHKWQYVANNLHEDLVIEVGLIKMNSSM |
Full Sequence |
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Protein Sequence Length: 555 Download |
MKSPCSSVIP LVFLLLLSYN SWVSYANVHA TSSKPADHHD ENLFLDCLSM HPDNSSSISQ 60 VIYTKYSPSY SSVLSSSAQN LRFSTPNTPK PQVIITPLDV SQVQAAIKCS KKHGFQIRVR 120 SGGHDFEGLS YVSQVPFVVI DLINLSKISV DAKQKTAWVQ SGATLGQLYY RIADKSKNLG 180 FPGGVCPTVG VGGHFSGGGY GIMLRKFGLA ADNIVDAHLI DARGRLLDRK SMGQDLFWAI 240 RGGGGTSFGV VVAWKLRLVT VPSTVTRFRI TRTLEQNATK IVHKWQYVAN NLHEDLVIEV 300 GLIKMNSSMV AVFSSLFLGG VDRLLPLMQE SFPELGLKKG DCTEMSWIES VHNLAGFDKG 360 QSLDLLLDRN ARSNGLVVKS TTKSPFKAKV DYVKQPIPEN AFEGIYDKFY EEEGETAFIV 420 LVPYGGKMSE ISESETPFPH RAGNLYKIFY GVSWRGDGIS QRHIDWIRSL YSYMTPYVSK 480 NPREAYVNYR DLDIGTNNQG YTSIEQASIW GNKYFKNNFK RLVHVKTMVD PHNFFRNEQS 540 IPPLTSWRKK NDGD* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 3.0e-17 | 485 | 542 | 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 | 1.0e-17 | 91 | 285 | 203 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 4.0e-21 | 91 | 228 | 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 |
RefSeq | XP_002299045.1 | 0 | 6 | 547 | 6 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002330610.1 | 0 | 1 | 547 | 1 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333020.1 | 0 | 1 | 547 | 1 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333338.1 | 0 | 1 | 547 | 1 | 533 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002333339.1 | 0 | 1 | 547 | 1 | 533 | 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 | 3vte_A | 0 | 44 | 544 | 7 | 513 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 4dns_B | 0 | 35 | 544 | 4 | 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 | 35 | 544 | 4 | 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 | 35 | 544 | 5 | 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 | 35 | 544 | 5 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |