| Basic Information | |
|---|---|
| Species | Zea mays |
| Cazyme ID | GRMZM2G080907_T01 |
| Family | AA7 |
| Protein Properties | Length: 547 Molecular Weight: 59940.9 Isoelectric Point: 8.7636 |
| Chromosome | Chromosome/Scaffold: 9 Start: 77179962 End: 77182089 |
| 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 | 100 | 332 | 0 |
| TVKPVYIITPTEAAHIQATVACGRKHGLRVRVRSGGHDYEGLSYRSAKPETFAVVDLSMMRQVRIDGKAATAWVDSGAQLGELYYAVAKMTPSLGFPAGV CATIGVGGHFSGGGFGMLLRKYGTAGDNVIDAKVVDANGTLLDRKSMGEDYFWAIRGGGGESFGIVVSWQVQLVPVPPKVTVFQIHRGVKDGAIDLINKW QQVAPSLPDDLMIRIMAMEQDAMFEALYLGTCK | |||
| Full Sequence |
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| Protein Sequence Length: 547 Download |
| MSCSCGDQTR TRCSAIHSPA MATSRPLALA LLFCALSACS HAAISYPPSA MSTAAPANNG 60 FLSCLIKSVP PRLLHGKSSR AYGSIWESTV RNVKFVSDKT VKPVYIITPT EAAHIQATVA 120 CGRKHGLRVR VRSGGHDYEG LSYRSAKPET FAVVDLSMMR QVRIDGKAAT AWVDSGAQLG 180 ELYYAVAKMT PSLGFPAGVC ATIGVGGHFS GGGFGMLLRK YGTAGDNVID AKVVDANGTL 240 LDRKSMGEDY FWAIRGGGGE SFGIVVSWQV QLVPVPPKVT VFQIHRGVKD GAIDLINKWQ 300 QVAPSLPDDL MIRIMAMEQD AMFEALYLGT CKDLLPLMAS RFPELGVKQE DCNEMPWIQS 360 VAFIPMGKSA TVMDLLNRTS NIKAFGKYKS DYVKDPIPRD VWEKIYTWLA KPGAGVMIMD 420 PYGARISSIP KDATPFPHRQ GVLFNIQYVS YWFGEGDGAA PTQWSRDMYA FMEPYVSKNP 480 RQAYANYRDL DLGVNEVVGD VSTYDSGRVW GEKYYNGNFE RLARTKAKVD PCDYFRNEQS 540 IPPLLK* |
| Functional Domains Download unfiltered results here | ||||||||
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| Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
| PLN02805 | PLN02805 | 0.004 | 103 | 330 | 256 | + D-lactate dehydrogenase [cytochrome] | ||
| pfam08031 | BBE | 5.0e-16 | 483 | 542 | 60 | + 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-20 | 97 | 544 | 480 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
| pfam01565 | FAD_binding_4 | 3.0e-23 | 103 | 242 | 141 | + 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 | |
|---|---|
| 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 | AAS02108.1 | 0 | 21 | 545 | 1 | 522 | FAD-linked oxidoreductase BG60 [Cynodon dactylon] |
| EMBL | CAH92630.1 | 0 | 23 | 545 | 1 | 518 | pollen allergen Sec c 4 [Secale cereale] |
| EMBL | CAH92635.1 | 0 | 23 | 545 | 1 | 516 | pollen allergen Hor v 4 [Hordeum vulgare] |
| RefSeq | NP_001148634.1 | 0 | 21 | 546 | 1 | 526 | reticuline oxidase [Zea mays] |
| RefSeq | XP_002438540.1 | 0 | 21 | 546 | 1 | 526 | hypothetical protein SORBIDRAFT_10g021680 [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 | 61 | 545 | 13 | 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 | 61 | 545 | 13 | 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 | 46 | 546 | 2 | 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 | 46 | 546 | 2 | 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 | 46 | 546 | 2 | 498 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
