y
Basic Information | |
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Species | Panicum virgatum |
Cazyme ID | Pavirv00019648m |
Family | AA7 |
Protein Properties | Length: 521 Molecular Weight: 54752.3 Isoelectric Point: 9.9212 |
Chromosome | Chromosome/Scaffold: 027594 Start: 401 End: 1971 |
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 | 86 | 321 | 0 |
LPGVRKPAAVVLPASRRDLRRAAIRVRSGGHSYEGQSYTVAGAALGGGDAPFVVIDLMNLNRVRADDASATAWAESGATLGEVYHAVARSASPNGSSSSS LAFSAGSCSTVGVGGHVSGGGFGLLSRKFMLAADNVLDALLVDAGPGPGAMGEDVFWAIRGGGGGSWGVVYAWKLRLVPVPDTGTVFTPRREGSVDAVAG LVHRWQFVGPALPDEFYLTVFLTISGASQEDTNVTV |
Full Sequence |
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Protein Sequence Length: 521 Download |
MMNTMTPTIC SRNPTALLFP GLILSFLLLS TRHNAAASEN GSVHAGASRS LASCLVASGV 60 RNFSLAGSPG YASLLGFSVQ NLRFALPGVR KPAAVVLPAS RRDLRRAAIR VRSGGHSYEG 120 QSYTVAGAAL GGGDAPFVVI DLMNLNRVRA DDASATAWAE SGATLGEVYH AVARSASPNG 180 SSSSSLAFSA GSCSTVGVGG HVSGGGFGLL SRKFMLAADN VLDALLVDAG PGPGAMGEDV 240 FWAIRGGGGG SWGVVYAWKL RLVPVPDTGT VFTPRREGSV DAVAGLVHRW QFVGPALPDE 300 FYLTVFLTIS GASQEDTNVT VSFTGLVLGP RELAMSVLSE RFPELGLAER ELSEMSWVES 360 AAQFAGLSSP EELTSRVSQT KHYGKNKSDY VRQPVARDAL AAILRYLSAG PAGYVILDPY 420 GGAMARAGAT DTPSPHRAGV QYGVTWEAGE DGEARMAWLR ALYAYMAPHV SGGPRAQWRT 480 QLFIKTRAKS QRPKLTHTLT AVKFVQNKIA KSRSSSLCKL * 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 0.003 | 113 | 172 | 61 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 7.0e-6 | 113 | 171 | 60 | + 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 |
DDBJ | BAD03275.1 | 0 | 47 | 478 | 27 | 481 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
DDBJ | BAF23509.2 | 0 | 47 | 478 | 31 | 485 | Os08g0343600 [Oryza sativa Japonica Group] |
GenBank | EAZ05659.1 | 0 | 23 | 482 | 8 | 466 | hypothetical protein OsI_27886 [Oryza sativa Indica Group] |
RefSeq | NP_001061595.1 | 0 | 47 | 478 | 35 | 489 | Os08g0343600 [Oryza sativa (japonica cultivar-group)] |
RefSeq | NP_001140781.1 | 0 | 49 | 482 | 34 | 486 | hypothetical protein LOC100272856 [Zea mays] |
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 | 45 | 475 | 21 | 453 | A Chain A, Human Artd15PARP16 IN COMPLEX WITH 3-Aminobenzamide |
PDB | 3d2h_A | 0 | 45 | 475 | 21 | 453 | A Chain A, Human Artd15PARP16 IN COMPLEX WITH 3-Aminobenzamide |
PDB | 3d2d_A | 0 | 45 | 475 | 21 | 453 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 4ec3_A | 0 | 44 | 475 | 1 | 434 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3gsy_A | 0 | 44 | 475 | 1 | 434 | 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 |