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Basic Information | |
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Species | Malus domestica |
Cazyme ID | MDP0000268860 |
Family | AA7 |
Protein Properties | Length: 695 Molecular Weight: 78121.2 Isoelectric Point: 9.4733 |
Chromosome | Chromosome/Scaffold: 000845305 Start: 13930 End: 17273 |
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 | 1 | 153 | 1.9e-32 |
MMRKYGLGADNAIDARIIDVNGQILDRKAMGEDLFWAIRGGGGASFGIILWWKIKLVSVPANVTVFSVAKTLEQGATKLLHRWQHVAPFLDEDLFIRVLL QVSNDTITASKTVTTVYQAHFLGDSKRLLNVMQKSFPELGLTRKDCTKTSWIE | |||
AA7 | 298 | 476 | 0 |
LYIITPYLYEHVQAAIICSKIHRLQVRIRSGGHDYEALSYKADVPFIIIDLVKLNKVKVNRGKRTAWVQSGATLGELYYHVANESRGKLGFTAGVCPTIG VGGHISGGGQGVLMRKFGLSSDNAVDAIVVTADGAVVDRQSMGEDLFWAIRGGGAASFGVVLEWKIKLAPVPPKANFNA |
Full Sequence |
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Protein Sequence Length: 695 Download |
MMRKYGLGAD NAIDARIIDV NGQILDRKAM GEDLFWAIRG GGGASFGIIL WWKIKLVSVP 60 ANVTVFSVAK TLEQGATKLL HRWQHVAPFL DEDLFIRVLL QVSNDTITAS KTVTTVYQAH 120 FLGDSKRLLN VMQKSFPELG LTRKDCTKTS WIESVLYIAG YPSGTPTEIL LEGKATLPKV 180 YFKAKSDFVK NPIPEIALKG LWKRLLEEPS PLMILNPYGG MMSKISESAI PFPHRKVLFK 240 IQYATVWQAG DNESKHMDWQ AYVNYRDLDL GSNKKSNTSF IEASSWGYRF NSTNQKLLYI 300 ITPYLYEHVQ AAIICSKIHR LQVRIRSGGH DYEALSYKAD VPFIIIDLVK LNKVKVNRGK 360 RTAWVQSGAT LGELYYHVAN ESRGKLGFTA GVCPTIGVGG HISGGGQGVL MRKFGLSSDN 420 AVDAIVVTAD GAVVDRQSMG EDLFWAIRGG GAASFGVVLE WKIKLAPVPP KANFNALFLG 480 TTDQLVPLMQ KSFPELGLKP EDCKEISWIQ SIFYINGEDP GQPLELLLDR NHVQKGFFKA 540 KSDFVTKPIS EKHLEAIWKV MQDGDVPGIM IWDPYGGQMA EIPEDFTPFP HRAGVLYNIQ 600 YFTKWFEGGA LAEKKHLEGI NRVYNFMAPF VTKNPRAAYI NYRDLDIGRN IKGTLEEAKV 660 WGEKYFKRNF ERLAKIKGEV DYENFFKSEQ NFVPI 720 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 0.0008 | 3 | 83 | 88 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 3.0e-13 | 638 | 691 | 54 | + 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 | 3.0e-15 | 298 | 488 | 198 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-16 | 298 | 435 | 139 | + 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 | |
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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_002268281.1 | 0 | 1 | 301 | 184 | 497 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002268281.1 | 0 | 276 | 695 | 52 | 516 | PREDICTED: hypothetical protein [Vitis vinifera] |
RefSeq | XP_002523164.1 | 0 | 1 | 294 | 194 | 505 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523164.1 | 0 | 299 | 469 | 82 | 253 | Reticuline oxidase precursor, putative [Ricinus communis] |
RefSeq | XP_002523164.1 | 0 | 473 | 695 | 309 | 531 | Reticuline oxidase precursor, putative [Ricinus communis] |
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 | 4dns_B | 0 | 296 | 695 | 54 | 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_B | 0 | 1 | 294 | 169 | 470 | 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 | 296 | 695 | 54 | 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 | 1 | 294 | 169 | 470 | 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 | 281 | 695 | 40 | 496 | A Chain A, Crystal Structure Of Bermuda Grass Isoallergen Bg60 Provides Insight Into The Various Cross-Allergenicity Of The Pollen Group 4 Allergens |
EST Download unfiltered results here | ||||
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Hit | Length | Start | End | EValue |
HO777438 | 484 | 275 | 695 | 0 |
HO777438 | 325 | 1 | 298 | 0 |
GR924372 | 293 | 1 | 274 | 0 |
GR924372 | 291 | 410 | 650 | 0 |
CX668319 | 249 | 1 | 247 | 0 |
Orthologous Group | |||||
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Species | ID | ||||
Citrus clementina | Ciclev10002058m | Ciclev10017593m | Ciclev10018258m | ||
Citrus sinensis | orange1.1g045207m | ||||
Malus domestica | MDP0000268860.298.476 | MDP0000268860.298.476 |
Sequence Alignments (This image is cropped. Click for full image.) |
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