| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G031941_T01 |
| Family | AA7 |
| Protein Properties | Length: 532 Molecular Weight: 58335.4 Isoelectric Point: 8.8315 |
| Chromosome | Chromosome/Scaffold: 9 Start: 77307280 End: 77309060 |
| Description | FAD-binding Berberine family protein |
| View CDS | |
| External Links |
|---|
| NCBI Taxonomy |
| CAZyDB |
| Signature Domain Download full data set without filtering | |||
|---|---|---|---|
 | |||
| Family | Start | End | Evalue |
| AA7 | 66 | 519 | 0 |
| NLRYVTSDIQRPVAIVAATEPAHAQAAVRCGRRHGVRVRARSGGHDYEGLSYASLDPGERFAVLDLAAFRDVRVDSARAEAWAGSGATLGEVYYAVAAAS RVLAFPAGICPTVGVGGHLSGGGFGTLMRRYGLAADNVIDAVLVDADGRLLNRTTMGEDLFWAIRGGGGESFGVVLSWKLRLVRVPETVTVFTVRRSINQ SASHLITKWQAIAPALPSDLILRVAVRSQHARFEALFLGRCSRLLEHMRVHFPDLGVTQSDCEEISWIQSTVYFAFYSSSKPLELLLDRSGETPRYVKAK SDYVQEPIPRHVWERTWSWLEKPEAGLLILDPYGGRMGSISPSATPFPHRKGNLYNLQYYSYWFENGTAALEKRMSWVRGLYEEMEPYVSKNPRTGYVNY RDLDLGTNELEDNVTSYARARIWGEKYFKGNFERLAAVKAMADPNDFFRNEQSI | |||
| Full Sequence |
|---|
| Protein Sequence Length: 532 Download |
| MPGILYQLVV AAAICALSSG SIAVASGLNA TDSFLVCLVG AGVPPRLLQT PASPSYSTTL 60 LSSVRNLRYV TSDIQRPVAI VAATEPAHAQ AAVRCGRRHG VRVRARSGGH DYEGLSYASL 120 DPGERFAVLD LAAFRDVRVD SARAEAWAGS GATLGEVYYA VAAASRVLAF PAGICPTVGV 180 GGHLSGGGFG TLMRRYGLAA DNVIDAVLVD ADGRLLNRTT MGEDLFWAIR GGGGESFGVV 240 LSWKLRLVRV PETVTVFTVR RSINQSASHL ITKWQAIAPA LPSDLILRVA VRSQHARFEA 300 LFLGRCSRLL EHMRVHFPDL GVTQSDCEEI SWIQSTVYFA FYSSSKPLEL LLDRSGETPR 360 YVKAKSDYVQ EPIPRHVWER TWSWLEKPEA GLLILDPYGG RMGSISPSAT PFPHRKGNLY 420 NLQYYSYWFE NGTAALEKRM SWVRGLYEEM EPYVSKNPRT GYVNYRDLDL GTNELEDNVT 480 SYARARIWGE KYFKGNFERL AAVKAMADPN DFFRNEQSIP PLPAAKGWGS I* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
 | ||||||||
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| pfam01565 | FAD_binding_4 | 4.0e-10 | 77 | 217 | 142 | + 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 | 4.0e-12 | 128 | 522 | 413 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam08031 | BBE | 9.0e-18 | 462 | 520 | 59 | + 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 | |
|---|---|
| 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 | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| DDBJ | BAD54128.1 | 0 | 8 | 531 | 14 | 535 | putative CPRD2 [Oryza sativa Japonica Group] |
| GenBank | EAZ01285.1 | 0 | 8 | 531 | 14 | 500 | hypothetical protein OsI_23309 [Oryza sativa Indica Group] |
| GenBank | EEE65853.1 | 0 | 8 | 531 | 14 | 513 | hypothetical protein OsJ_21632 [Oryza sativa Japonica Group] |
| RefSeq | NP_001057826.1 | 0 | 8 | 531 | 1225 | 1746 | Os06g0548100 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | NP_001143977.1 | 0 | 1 | 531 | 1 | 531 | hypothetical protein LOC100276794 [Zea mays] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4dns_B | 0 | 33 | 522 | 12 | 496 | 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 | 33 | 522 | 12 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_B | 0 | 30 | 522 | 7 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsj_A | 0 | 30 | 522 | 7 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
| PDB | 3tsh_A | 0 | 30 | 522 | 7 | 496 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
