y
Basic Information | |
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Species | Zea mays |
Cazyme ID | GRMZM2G173105_T01 |
Family | AA7 |
Protein Properties | Length: 544 Molecular Weight: 59243.5 Isoelectric Point: 8.2695 |
Chromosome | Chromosome/Scaffold: 4 Start: 17740852 End: 17742683 |
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 | 85 | 538 | 0 |
NTTVRPLCIITASDVSHVQTAVRCGRWNGVRLRVRSGGHDYEGLSYRSVQPEVFAVLDLARLRGVQVRPGDDSAWVDAGTTLGELYYAVGTTNPGFLFPG GACATVGVSGFISGGGIGLMMRKYGVGGDNVVDARIVNANGDVLDRFAMGDDLFWAIRGGGGETFGVVVAWRLKLSKVPPTVTVVNVLRTMEQGAADLVA KWETTILQPPVLPDLTIRVVLQYRQAFFQTLFLGGCSDLLNTMRGLFPELGTTAADCHEMSWLRAMAFIYFGNTDTPVEALLNRTNNVGNYYFKSKSDYV RRAVGKAGWDSLYQQWLSQNGNGQIILEPHGAAVGGANTMTTSPYPHRRGVLFNIQYGSNWCCGANGTEAAAALGWLNGLYGFMAQFVTSNPREAFANYR DLDMGQNVIGSDGLSSYWSARAWAERYFMGNYRRLAAVKAAVDPTDYFRNEQSI |
Full Sequence |
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Protein Sequence Length: 544 Download |
MQPIERSMQQ YHRSTMAASG RKAVVVLILC MLCCNTSLLP CSASSDSFLQ CLSAMMPSEL 60 VYQQSSSSFT SVLQSSVQNP KFVTNTTVRP LCIITASDVS HVQTAVRCGR WNGVRLRVRS 120 GGHDYEGLSY RSVQPEVFAV LDLARLRGVQ VRPGDDSAWV DAGTTLGELY YAVGTTNPGF 180 LFPGGACATV GVSGFISGGG IGLMMRKYGV GGDNVVDARI VNANGDVLDR FAMGDDLFWA 240 IRGGGGETFG VVVAWRLKLS KVPPTVTVVN VLRTMEQGAA DLVAKWETTI LQPPVLPDLT 300 IRVVLQYRQA FFQTLFLGGC SDLLNTMRGL FPELGTTAAD CHEMSWLRAM AFIYFGNTDT 360 PVEALLNRTN NVGNYYFKSK SDYVRRAVGK AGWDSLYQQW LSQNGNGQII LEPHGAAVGG 420 ANTMTTSPYP HRRGVLFNIQ YGSNWCCGAN GTEAAAALGW LNGLYGFMAQ FVTSNPREAF 480 ANYRDLDMGQ NVIGSDGLSS YWSARAWAER YFMGNYRRLA AVKAAVDPTD YFRNEQSIPP 540 LPK* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
PLN02805 | PLN02805 | 0.0006 | 179 | 263 | 100 | + D-lactate dehydrogenase [cytochrome] | ||
pfam08031 | BBE | 2.0e-13 | 479 | 539 | 61 | + 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. | ||
pfam01565 | FAD_binding_4 | 5.0e-18 | 90 | 229 | 143 | + 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 | 9.0e-20 | 87 | 296 | 229 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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 |
GenBank | ABA93766.1 | 0 | 20 | 541 | 8 | 536 | Reticuline oxidase precursor, putative [Oryza sativa (japonica cultivar-group)] |
DDBJ | BAD53690.1 | 0 | 16 | 541 | 1 | 519 | putative CPRD2 [Oryza sativa Japonica Group] |
GenBank | EAY80999.1 | 0 | 20 | 541 | 8 | 536 | hypothetical protein OsI_36182 [Oryza sativa Indica Group] |
RefSeq | NP_001067934.1 | 0 | 20 | 506 | 8 | 501 | Os11g0495700 [Oryza sativa (japonica cultivar-group)] |
RefSeq | XP_002438541.1 | 0 | 23 | 540 | 8 | 522 | hypothetical protein SORBIDRAFT_10g021685 [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 | 3tsj_B | 0 | 39 | 543 | 2 | 498 | V Chain V, Crystallographic Structure Of A Putative Chlorite Dismutase |
PDB | 3tsj_A | 0 | 39 | 543 | 2 | 498 | V Chain V, Crystallographic Structure Of A Putative Chlorite Dismutase |
PDB | 3tsh_A | 0 | 39 | 543 | 2 | 498 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
PDB | 4dns_B | 0 | 47 | 541 | 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 | 47 | 541 | 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 |