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Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 1294 |
Family | AA7 |
Protein Properties | Length: 548 Molecular Weight: 60253.8 Isoelectric Point: 6.6656 |
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 | 102 | 317 | 0 |
VYAVNVSHVFQVELAVAFASKHNLLLVVKNTGHDYLGRSTARGSLSIWMHHLRELRFHGDLGCDQAEHCDDLGLDPAAYVTIGAGVTWNQLYEAALEHRR DIVGASCPWVGAAGGFAQGGGHSLLSPVFGLAADNVVELQVVTADGKRKVASECQNEDLFWALRGGGGGTFGVVVSLTYRTYPALENAIFASVNVTAKDR PSFETLLEEFARMNPE |
Full Sequence |
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Protein Sequence Length: 548 Download |
SSCRCLHGDP NCWPQDRDWK IFNASIQGRL IAVKPPAWPC HDPQYDHHLC ELATENWSDP 60 TWRSDQPGAM MADNWEMDDA RNESCSIRDP RSSRCEQGSV PVYAVNVSHV FQVELAVAFA 120 SKHNLLLVVK NTGHDYLGRS TARGSLSIWM HHLRELRFHG DLGCDQAEHC DDLGLDPAAY 180 VTIGAGVTWN QLYEAALEHR RDIVGASCPW VGAAGGFAQG GGHSLLSPVF GLAADNVVEL 240 QVVTADGKRK VASECQNEDL FWALRGGGGG TFGVVVSLTY RTYPALENAI FASVNVTAKD 300 RPSFETLLEE FARMNPELSS DGWSGFFNVG NFSLSLRYVL PNKTLAFARS SLNFLLGFQH 360 NRIQTHYSLK SYASFYELIQ QALCGSDPSC PNVGGLAGNP VLPASRLIPT QALNSFPTKV 420 SRALAKIALD FQVPIVGAFV AGGQVSVPRD SAVNPAWRDS LWLVIVSVSA PRSQRKEAAT 480 LVSRANKVLI DITPGSGSYM NEADYNEPHF HRSFFGSHYK RLYEIKQRVD PGGLFVCHHC 540 VGSEDWTQ 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 4.0e-7 | 498 | 535 | 38 | + 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 | 1.0e-13 | 112 | 535 | 454 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam01565 | FAD_binding_4 | 2.0e-14 | 101 | 253 | 156 | + 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. |
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 | 3rja_A | 0.00000000001 | 88 | 541 | 24 | 469 | A Chain A, Crystal Structure Of A Putative Dipeptidyl-Peptidase Vi (Bacova_00612) From Bacteroides Ovatus At 1.72 A Resolution |
PDB | 3rj8_A | 0.00000000001 | 88 | 541 | 24 | 469 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 3tsj_B | 0.00000000004 | 86 | 321 | 39 | 259 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 3tsj_A | 0.00000000004 | 86 | 321 | 39 | 259 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 3tsh_A | 0.00000000004 | 86 | 321 | 39 | 259 | A Chain A, Crystal Structure Of Phl P 4, A Grass Pollen Allergen With Glucose Dehydrogenase Activity |
Sequence Alignments (This image is cropped. Click for full image.) |
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