| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G429540_T02 |
| Family | AA7 |
| Protein Properties | Length: 488 Molecular Weight: 52216.6 Isoelectric Point: 9.3859 |
| Chromosome | Chromosome/Scaffold: 5 Start: 146883825 End: 146885510 |
| 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 | 85 | 313 | 0 |
| PRTPRPALLLTPATVAEARACVTCCRRHGLTVRARSGGHDYEGLSYRSVAGARPFAVVDVAALRDVRVDAGRRVARAGPGATLGELYYAVTRESGGALGF PAGICPTVCVGGHLSGGGFGPMMRKHGLGADNVVDAEVVDAEGRLLDRAAMGEGLFWAIRGGGGGSFGVVVSWTVRLVPVPPVVSAFTVRRLVRRGDQRQ TQAAVRLLTKWQRVAHALPEDLFVKVAME | |||
| Full Sequence |
|---|
| Protein Sequence Length: 488 Download |
| MMSKTKAAVR PRSWHLPFLF LLLLAQTCSP QEQGGGGALH GSFVRCVARL SPATTDTSRL 60 VHAPSAASYP SLLNATIQNL RFASPRTPRP ALLLTPATVA EARACVTCCR RHGLTVRARS 120 GGHDYEGLSY RSVAGARPFA VVDVAALRDV RVDAGRRVAR AGPGATLGEL YYAVTRESGG 180 ALGFPAGICP TVCVGGHLSG GGFGPMMRKH GLGADNVVDA EVVDAEGRLL DRAAMGEGLF 240 WAIRGGGGGS FGVVVSWTVR LVPVPPVVSA FTVRRLVRRG DQRQTQAAVR LLTKWQRVAH 300 ALPEDLFVKV AMEPEVDDAG ERHPSVTFKS LFLGNCSGMV AEMSAHLTSP IPAAGLGGLL 360 ARVVEDRGGS VDVDPQGGAM SETPESDTPY AHRRGYLAWV RGVHRFMTPY ASARPRAAYV 420 NFRDLDLGQN LEGETSYEAA RAWGEMYFRG NFRRLAMVKA EVDPDQVFWS EQSIPPLLQT 480 NGMLSDT* 540 |
| Functional Domains Download unfiltered results here | ||||||||
|---|---|---|---|---|---|---|---|---|
| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| COG0277 | GlcD | 0.007 | 99 | 477 | 442 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 7.0e-11 | 99 | 231 | 133 | + 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 | 2.0e-17 | 418 | 475 | 58 | + 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 |
| GenBank | ACL54298.1 | 0 | 1 | 487 | 1 | 487 | unknown [Zea mays] |
| GenBank | ACN34780.1 | 0 | 1 | 487 | 1 | 561 | unknown [Zea mays] |
| GenBank | EAY85134.1 | 0 | 25 | 487 | 21 | 566 | hypothetical protein OsI_06489 [Oryza sativa Indica Group] |
| RefSeq | NP_001046387.1 | 0 | 23 | 478 | 20 | 555 | Os02g0235900 [Oryza sativa (japonica cultivar-group)] |
| RefSeq | XP_002451843.1 | 0 | 7 | 469 | 2 | 548 | hypothetical protein SORBIDRAFT_04g008542 [Sorghum bicolor] |
| Annotations - PDB Download unfiltered results here | |||||||
|---|---|---|---|---|---|---|---|
| Source | Hit ID | E-Value | Query Start | Query End | Hit Start | Hit End | Description |
| PDB | 4dns_B | 0 | 42 | 478 | 12 | 497 | 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 | 42 | 478 | 12 | 497 | 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 | 43 | 479 | 11 | 498 | 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 | 43 | 479 | 11 | 498 | 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 | 43 | 479 | 11 | 498 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
