Basic Information | |
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Species | Eucalyptus grandis |
Cazyme ID | Eucgr.D00075.1 |
Family | AA7 |
Protein Properties | Length: 541 Molecular Weight: 60031.6 Isoelectric Point: 6.6765 |
Chromosome | Chromosome/Scaffold: 4 Start: 1144873 End: 1146793 |
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 | 71 | 528 | 0 |
RNLRFNSSTTPKPLFIVTPTHVSHIQASVVCAKIHGLELRIRSGGHDYDGLSYVSPAPFVIVDMFNLRSVDIDAEGGTAWVESGATLGEVYYAIAARSGV HAFPAGVCPTVGVGGHLSGGGYGNLMRKHGLSVDNVVDAVVVDANGRVLDRGSMGDDMFWAIRGGGGASFGVIVSWKIKLVSVPEVVTVFKVEKTLEQGA TDVVHRWQYVADKVDERLFIRVVLLPVVRKDQRTVKAKFVALFLGGADELLDVMSQSFPEFGLEPKDCLEMSWIESVLFWSNYPKGTSPNVLLQRIPESE KFLKKKSDYVQEPISKVGLEGIWNKMMELKRPALTLNPYGGRMSEISDSETPFPHREGNIFKIQYSVTWKEEGDEALNQNLNRIRSIYNHMTPFVAKSPR SSYLNYRDTDLGINQIGNESYSEASIWGTKYFKANFDRLVQVKTMVDPNNFFRYEQSI |
Full Sequence |
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Protein Sequence Length: 541 Download |
MNLPCFCPVL LLALQASLLS SSMAESPQDR TQETYLQCLI DSSDPSSPPI SPLAFFPSNP 60 SYSSVLRSYV RNLRFNSSTT PKPLFIVTPT HVSHIQASVV CAKIHGLELR IRSGGHDYDG 120 LSYVSPAPFV IVDMFNLRSV DIDAEGGTAW VESGATLGEV YYAIAARSGV HAFPAGVCPT 180 VGVGGHLSGG GYGNLMRKHG LSVDNVVDAV VVDANGRVLD RGSMGDDMFW AIRGGGGASF 240 GVIVSWKIKL VSVPEVVTVF KVEKTLEQGA TDVVHRWQYV ADKVDERLFI RVVLLPVVRK 300 DQRTVKAKFV ALFLGGADEL LDVMSQSFPE FGLEPKDCLE MSWIESVLFW SNYPKGTSPN 360 VLLQRIPESE KFLKKKSDYV QEPISKVGLE GIWNKMMELK RPALTLNPYG GRMSEISDSE 420 TPFPHREGNI FKIQYSVTWK EEGDEALNQN LNRIRSIYNH MTPFVAKSPR SSYLNYRDTD 480 LGINQIGNES YSEASIWGTK YFKANFDRLV QVKTMVDPNN FFRYEQSIPC MSSWPSRMAE 540 * |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 1.0e-10 | 64 | 350 | 311 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 3.0e-17 | 83 | 222 | 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 | 472 | 529 | 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. |
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 | CAN72775.1 | 0 | 14 | 540 | 12 | 509 | hypothetical protein [Vitis vinifera] |
EMBL | CBI31067.1 | 0 | 10 | 540 | 8 | 517 | unnamed protein product [Vitis vinifera] |
RefSeq | XP_002268682.1 | 0 | 10 | 540 | 8 | 535 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002300580.1 | 0 | 29 | 540 | 5 | 517 | predicted protein [Populus trichocarpa] |
RefSeq | XP_002523156.1 | 0 | 29 | 533 | 5 | 509 | 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 | 30 | 529 | 8 | 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 | 529 | 8 | 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 | 32 | 529 | 4 | 511 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_B | 0 | 27 | 531 | 3 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |
PDB | 3tsj_A | 0 | 27 | 531 | 3 | 496 | A Chain A, Crystal Structure Of Tetrahydrocannabinolic Acid Synthase From Cannabis Sativa |