Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00068789m |
Family | AA7 |
Protein Properties | Length: 542 Molecular Weight: 57789.4 Isoelectric Point: 8.9984 |
Chromosome | Chromosome/Scaffold: 009463 Start: 4258 End: 5888 |
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 | 531 | 0 |
RFELQGVGKPAAVILPGSERDLRRAVLCARRAALAIRVRSGGHSYEGLSYTSENRVPFAVIDLASLNSVRVDPGSATVWAEAGATLGELYHAVGRSSRTL ALPAGSCATMGVGGHVAGGGFGLLSRKHGLAADNVLDAVLIDPSGRTLTRDTMDADVFWAIRGGGGGSWGVVYAWKLRLVPVPDTITVFTVRRTGPAELI AGLMYRWQYVAPSLPDEFYLSTYIPTGSSPDGNLSMSFTGQVLGPKHLAMSVLDQTFPALGLAEAGSPSWLESAANFAGLRSVADLTNRQPGAGEYAKSK SDYVRAPISMQGATRILRHMSTGPPGSIQLDPYGGAMARVGSGATPFPHRAGHLYSIQYAVTWNASDHRLGRAEERIGWLRSFHEFMARYVSRNPRRAYV NYLDLDLGTNGWANATGGTSGESVARAASWGERYFFTNFDRLVRAKTKVDPENVFNNAQSI |
Full Sequence |
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Protein Sequence Length: 542 Download |
MAMHTMATAA AALALCLFAA AATCAGAQPP PPLQAYDDIS SCLLSNGVSN FSLPSSPSYT 60 PLLDSSIRNL RFELQGVGKP AAVILPGSER DLRRAVLCAR RAALAIRVRS GGHSYEGLSY 120 TSENRVPFAV IDLASLNSVR VDPGSATVWA EAGATLGELY HAVGRSSRTL ALPAGSCATM 180 GVGGHVAGGG FGLLSRKHGL AADNVLDAVL IDPSGRTLTR DTMDADVFWA IRGGGGGSWG 240 VVYAWKLRLV PVPDTITVFT VRRTGPAELI AGLMYRWQYV APSLPDEFYL STYIPTGSSP 300 DGNLSMSFTG QVLGPKHLAM SVLDQTFPAL GLAEAGSPSW LESAANFAGL RSVADLTNRQ 360 PGAGEYAKSK SDYVRAPISM QGATRILRHM STGPPGSIQL DPYGGAMARV GSGATPFPHR 420 AGHLYSIQYA VTWNASDHRL GRAEERIGWL RSFHEFMARY VSRNPRRAYV NYLDLDLGTN 480 GWANATGGTS GESVARAASW GERYFFTNFD RLVRAKTKVD PENVFNNAQS IPPLRHDDRE 540 H* |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 2.0e-13 | 75 | 534 | 481 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 3.0e-15 | 80 | 219 | 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 | 8.0e-16 | 468 | 532 | 65 | + 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 | EAZ05659.1 | 0 | 15 | 534 | 12 | 528 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
RefSeq | NP_001061035.1 | 0 | 42 | 535 | 36 | 529 | Os08g0158200 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001140781.1 | 0 | 39 | 534 | 36 | 548 | hypothetical protein LOC100272856 [Zea mays] |
RefSeq | XP_002445087.1 | 0 | 31 | 533 | 35 | 556 | hypothetical protein SORBIDRAFT_07g003930 [Sorghum bicolor] |
RefSeq | XP_002445088.1 | 0 | 38 | 509 | 43 | 519 | hypothetical protein SORBIDRAFT_07g003940 [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 | 3d2j_A | 0 | 13 | 538 | 9 | 523 | A Chain A, Crystal Structure Of Ilve A Branched Chain Amino Acid Transaminase From Mycobacterium Tuberculosis |
PDB | 3d2h_A | 0 | 13 | 538 | 9 | 523 | A Chain A, Crystal Structure Of Ilve A Branched Chain Amino Acid Transaminase From Mycobacterium Tuberculosis |
PDB | 3d2d_A | 0 | 13 | 538 | 9 | 523 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 4ec3_A | 0 | 34 | 538 | 3 | 504 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 34 | 538 | 3 | 504 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With Dehydroscoulerine |
Metabolic Pathways | |||
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Pathway Name | Reaction | EC | Protein Name |
berberine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
dehydroscoulerine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |