y
Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 437311 |
Family | AA7 |
Protein Properties | Length: 544 Molecular Weight: 58736.8 Isoelectric Point: 7.3763 |
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 | 163 | 268 | 8.7e-37 |
VTAQPGVTWKSLYDFLDRRGRVAVGPMASSLSAAGGFVQGGGHGPLSRTFGYAVDNTLELKVVTADGRVRVANQCQNPELFWALKGGGGGTFGVVVSTTY RTFPEL |
Full Sequence |
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Protein Sequence Length: 544 Download |
MEFFHPARLL LLLSILSPLS LLSSDGGHKC TPLSSCWPSS TLWSAFNRSI DGRLLAPKPY 60 AWPCHTPQYD PAACSAARQL QNNPFARSDV VGAMQTPTWE SGIAGLGCPL NGSGALSTPC 120 YQDQVSAYAI NVSSVSHVQA GVLFARKFNL RLSCPGCDPL PAVTAQPGVT WKSLYDFLDR 180 RGRVAVGPMA SSLSAAGGFV QGGGHGPLSR TFGYAVDNTL ELKVVTADGR VRVANQCQNP 240 ELFWALKGGG GGTFGVVVST TYRTFPELKL GYLHTLFIAA SSSPSSHRDL VAKFVEVTPS 300 MDEARLAGYF YIYTSLVIIS FVLPNGTVAE AQAAFAPLVS YVDKNPELLV INNTVTSHDT 360 FVQWQDGVLC AVNPVLCTDA TGTSGLFATR FMPKKIFQES PAVLTDTLMR VLFERNFSPI 420 FGLFVFGGAA SSVQGRNNAL SAVWREALWH VLIVRTWNES TSVEERYQFS RSLTSANGLF 480 RSITPGGGCY KNEGDYFEPY WEESFFGEKY STLKAIKESV DPTGLFLCWK CVGSESLVQG 540 GAS* 600 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
pfam08031 | BBE | 5.0e-6 | 489 | 526 | 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. | ||
pfam01565 | FAD_binding_4 | 8.0e-8 | 163 | 235 | 75 | + 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 | 4.0e-9 | 163 | 526 | 378 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] |
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 | 0.0000000003 | 100 | 532 | 4 | 469 | A Chain A, Crystal Structure Of Alpha-1,34-Fucosidase From Bifidobacterium Longum Subsp. Infantis Complexed With Deoxyfuconojirimycin |
PDB | 3rj8_A | 0.0000000003 | 100 | 532 | 4 | 469 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 2bvh_D | 0.0000003 | 198 | 526 | 137 | 448 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 2bvh_C | 0.0000003 | 198 | 526 | 137 | 448 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |
PDB | 2bvh_B | 0.0000003 | 198 | 526 | 137 | 448 | A Chain A, Crystal Structure Of Carbohydrate Oxidase From Microdochium Nivale |