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Basic Information | |
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Species | Physcomitrella patens |
Cazyme ID | Pp1s128_133V6.1 |
Family | AA7 |
Protein Properties | Length: 502 Molecular Weight: 54617.5 Isoelectric Point: 9.9712 |
Chromosome | Chromosome/Scaffold: 128 Start: 969653 End: 972375 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
Plaza |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 66 | 498 | 0 |
ARLAYNLRERYAPSAFVFPTTVAQVQNAVFCAKQVGVGIVPRGGGHSYEDYSLGGRDGVLVVDMEGFKQFSYNKAAKTAVVGAGFRLGPLYLALWNAGKV TIPAGNCPTVGIAGHALGGGWGFSSRKFGLVTDNILEVQLVAANGTVVTANAQKNKDLYFAIRGAGATSYGIVTQFTFRVHDVSAPVTHFKYRWNDKAVL FKNFKSFQSWGLNVPAEISAAFYMDPSGVSWLEGTYLGKKTSLLPLVKTFLASAAPNPTRVEEELNWIQLILVNWNYPSNTNPNQLNNVPFTTNTFKAKS IYVNGPGLSDAGINAMINAMNTGSNAYFIYDLYGSQSAINKVVPGETAFIHRNSLYSIQMVASWSNDNNAVTQTSYITRYWKVVRTYATGQAYQNYIDRD MPLSAYYGSSLSTLIAGKKKWDPQNVFNFPQSI |
Full Sequence |
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Protein Sequence Length: 502 Download |
MGLKFAVLRV TAALACVLMV LLMCFQPVAG NEQRMGRKLA ATTLKQCLAK GGARTAFPGT 60 SEYSTARLAY NLRERYAPSA FVFPTTVAQV QNAVFCAKQV GVGIVPRGGG HSYEDYSLGG 120 RDGVLVVDME GFKQFSYNKA AKTAVVGAGF RLGPLYLALW NAGKVTIPAG NCPTVGIAGH 180 ALGGGWGFSS RKFGLVTDNI LEVQLVAANG TVVTANAQKN KDLYFAIRGA GATSYGIVTQ 240 FTFRVHDVSA PVTHFKYRWN DKAVLFKNFK SFQSWGLNVP AEISAAFYMD PSGVSWLEGT 300 YLGKKTSLLP LVKTFLASAA PNPTRVEEEL NWIQLILVNW NYPSNTNPNQ LNNVPFTTNT 360 FKAKSIYVNG PGLSDAGINA MINAMNTGSN AYFIYDLYGS QSAINKVVPG ETAFIHRNSL 420 YSIQMVASWS NDNNAVTQTS YITRYWKVVR TYATGQAYQN YIDRDMPLSA YYGSSLSTLI 480 AGKKKWDPQN VFNFPQSIPL K* 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02805 | PLN02805 | 0.006 | 78 | 134 | 57 | + D-lactate dehydrogenase [cytochrome] | ||
pfam08031 | BBE | 3.0e-9 | 457 | 499 | 45 | + 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. | ||
pfam01565 | FAD_binding_4 | 1.0e-18 | 78 | 205 | 130 | + 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. | ||
COG0277 | GlcD | 6.0e-20 | 60 | 501 | 475 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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_001770677.1 | 0 | 1 | 501 | 406 | 906 | predicted protein [Physcomitrella patens subsp. patens] |
RefSeq | XP_001938664.1 | 0 | 44 | 498 | 29 | 490 | glucooligosaccharide oxidase [Pyrenophora tritici-repentis Pt-1C-BFP] |
RefSeq | XP_002148536.1 | 0 | 35 | 501 | 1 | 474 | glucooligosaccharide oxidase, putative [Penicillium marneffei ATCC 18224] |
RefSeq | YP_001252780.1 | 0 | 48 | 498 | 1 | 434 | FAD-binding protein [Clostridium botulinum A str. ATCC 3502] |
RefSeq | YP_001785568.1 | 0 | 48 | 498 | 1 | 434 | FAD-binding protein [Clostridium botulinum A3 str. Loch Maree] |
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 | 3rja_A | 0 | 44 | 501 | 3 | 473 | A Chain A, Crystal Structure Of 1,2-A-L-Fucosidase From Bifidobacterium Bifidum (Apo Form) |
PDB | 3rj8_A | 0 | 44 | 501 | 3 | 473 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 3tsj_B | 8e-35 | 25 | 499 | 2 | 494 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 3tsj_A | 8e-35 | 25 | 499 | 2 | 494 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 3tsh_A | 8e-35 | 25 | 499 | 2 | 494 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
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 |
dehydroscoulerine biosynthesis | RXN-10888 | EC-1.21.3 | reticuline oxidase |
sanguinarine and macarpine biosynthesis | RETICULINE-OXIDASE-RXN | EC-1.21.3.3 | reticuline oxidase |
Transmembrane Domains | |||||
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Start | End | ||||
7 | 29 |
Signal Peptide | |||||
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Cleavage Site | |||||
30 |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
FC450930 | 168 | 335 | 502 | 0 |
BY953955 | 125 | 1 | 125 | 0 |
BY975336 | 114 | 1 | 114 | 0 |
GO913670 | 143 | 33 | 175 | 0 |
BJ872295 | 247 | 236 | 478 | 0 |
Orthologous Group | |||||
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Species | ID | ||||
Physcomitrella patens | Pp1s85_169V6.1 |
Sequence Alignments (This image is cropped. Click for full image.) |
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