Basic Information | |
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Species | Oryza sativa |
Cazyme ID | LOC_Os08g06190.1 |
Family | AA7 |
Protein Properties | Length: 563 Molecular Weight: 60567.8 Isoelectric Point: 6.3377 |
Chromosome | Chromosome/Scaffold: 8 Start: 3415483 End: 3417171 |
Description | FAD-binding Berberine family protein |
View CDS |
External Links |
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NCBI Taxonomy |
CAZyDB |
Signature Domain Download full data set without filtering | |||
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Family | Start | End | Evalue |
AA7 | 70 | 534 | 0 |
VAKPAAVVVPATRGELRDAVRCAREAGLGAVRLRSGGHSYEGVSYTGEDDGGFVVVDLLALDGVRVDAASRTAWVESGATLGQVYQAVAAASPALAFSAG SCPTVGSGGHIAGGGFGFLSRKYGLAGDNVIDAVLIAADGRVLDRAGMGEDVFWAIRGGGGGTWGAVYAWRIQLVPVPERVTAFVVNRPGTAESVAELVA AWQHVAPWLPDEFYLSAFVGAGLPEMNRTGISVTFKGLYLGPAHEAVEILTARLPEIGLSDLNPIEMSWIESVVFFSGLPQGSSVSDLTDRVLHKKKYFK AKSDYVRRPMRIGELIRAIDLLSTEPKAYVILDPYGGAMDRIGSASLPFPHRRGNIHGIQYLIEWTANDDDHREEYMDWIRRFYEFMGSYVPNSPRTAYI NYMDLDLGMNNWSNLRMYGGDGIPNPEVEAARVWGERYFLGNYDRLVRAKTAIDPDNVFRNAQSI |
Full Sequence |
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Protein Sequence Length: 563 Download |
MAMAIATAAL LSLLAVLRAG GDVDDGGGAI MEPCLAAAGV RNVTARRERD AYDAALRASA 60 QNLRFAGDGV AKPAAVVVPA TRGELRDAVR CAREAGLGAV RLRSGGHSYE GVSYTGEDDG 120 GFVVVDLLAL DGVRVDAASR TAWVESGATL GQVYQAVAAA SPALAFSAGS CPTVGSGGHI 180 AGGGFGFLSR KYGLAGDNVI DAVLIAADGR VLDRAGMGED VFWAIRGGGG GTWGAVYAWR 240 IQLVPVPERV TAFVVNRPGT AESVAELVAA WQHVAPWLPD EFYLSAFVGA GLPEMNRTGI 300 SVTFKGLYLG PAHEAVEILT ARLPEIGLSD LNPIEMSWIE SVVFFSGLPQ GSSVSDLTDR 360 VLHKKKYFKA KSDYVRRPMR IGELIRAIDL LSTEPKAYVI LDPYGGAMDR IGSASLPFPH 420 RRGNIHGIQY LIEWTANDDD HREEYMDWIR RFYEFMGSYV PNSPRTAYIN YMDLDLGMNN 480 WSNLRMYGGD GIPNPEVEAA RVWGERYFLG NYDRLVRAKT AIDPDNVFRN AQSIPPLGSR 540 RMSRIPRGIS PKIASKDKTY DS* |
Functional Domains Download unfiltered results here | ||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description |
pfam01565 | FAD_binding_4 | 5.0e-16 | 81 | 213 | 134 | + 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 | 6.0e-17 | 467 | 535 | 69 | + 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 | 4.0e-17 | 84 | 537 | 473 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
Gene Ontology | |
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GO Term | Description |
GO:0003674 | molecular_function |
GO:0003824 | catalytic activity |
GO:0005488 | binding |
GO:0005623 | cell |
GO:0008152 | metabolic 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 | BAC65012.1 | 0 | 1 | 562 | 1 | 562 | putative berberine bridge enzyme [Oryza sativa Japonica Group] |
GenBank | EAZ05661.1 | 0 | 1 | 562 | 1 | 562 | hypothetical protein OsI_27888 [Oryza sativa Indica Group] |
GenBank | EAZ41578.1 | 0 | 242 | 562 | 42 | 362 | hypothetical protein OsJ_26112 [Oryza sativa Japonica Group] |
GenBank | EAZ41579.1 | 0 | 29 | 406 | 29 | 376 | hypothetical protein OsJ_26113 [Oryza sativa Japonica Group] |
RefSeq | XP_002445090.1 | 0 | 2 | 562 | 3 | 512 | hypothetical protein SORBIDRAFT_07g003960 [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 | 5 | 539 | 9 | 521 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3d2h_A | 0 | 5 | 539 | 9 | 521 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
PDB | 3d2d_A | 0 | 5 | 539 | 9 | 521 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Reticuline |
PDB | 3fw9_A | 0 | 34 | 538 | 5 | 495 | A Chain A, Structure Of Berberine Bridge Enzyme In Complex With (S)-Scoulerine |
PDB | 4ec3_A | 0 | 34 | 539 | 11 | 502 | A Chain A, Structure Of Berberine Bridge Enzyme, H174a Variant In Complex With (S)-Reticuline |
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 |