Basic Information | |
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Species | Selaginella moellendorffii |
Cazyme ID | 2240 |
Family | AA7 |
Protein Properties | Length: 539 Molecular Weight: 58188.2 Isoelectric Point: 6.9385 |
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 | 88 | 287 | 2.99878e-43 |
PVYAVNVSTPSHVQSAVRFASTKNIRLVIKNTGHDFFGKSTAAGSLSIWTHHLKNISFHHDFVAKRCSVSPVSAVTVGAGVQWEELYQAVFKQGKVIVGA GGVTVGAAGGYPQAAGHSPISPAFGLAADNVLEYEVVTAAGDLVVANGCQNEDLFWALRGGGGGTFGVVVSATHRTHPQLEDLAFAGYSINARDRSSFLD |
Full Sequence |
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Protein Sequence Length: 539 Download |
CWPDPSAWDT FNSSLDGRLI KVLPPAAPCH ESNFDEQACQ IVRERWSSPF WRSDQPGAMQ 60 ASNWEASGDQ SCLISSPRNS SCSQGSVPVY AVNVSTPSHV QSAVRFASTK NIRLVIKNTG 120 HDFFGKSTAA GSLSIWTHHL KNISFHHDFV AKRCSVSPVS AVTVGAGVQW EELYQAVFKQ 180 GKVIVGAGGV TVGAAGGYPQ AAGHSPISPA FGLAADNVLE YEVVTAAGDL VVANGCQNED 240 LFWALRGGGG GTFGVVVSAT HRTHPQLEDL AFAGYSINAR DRSSFLDLLT NFAVIHPSLS 300 EAGWSGYFGL SSQSLQVSYL LPNKDVSFAN RTLATFLDYV EKHPKLQGNG SVVSLSSFQE 360 YYSQFLCGGQ NSCVNSNGSA TPLLLSSRLI PKSLFHSRKS VEPLSDALVS ILERYPPPLT 420 IFGAFVAGGA VARPRDENAV NPAWRRALLF VIIGSGWRDG ASLEEQREVA RNVSAANKLL 480 IDVTPGSGTY INEADFNEPD WQQSFFGEHY PRLQAIKSKV DPSGLFRCHH CVGSEKWSN 540 |
Functional Domains Download unfiltered results here | ||||||||
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Cdd ID | Domain | E-Value | Start | End | Length | Domain Description | ||
COG0277 | GlcD | 7.0e-11 | 87 | 527 | 470 | + FAD/FMN-containing dehydrogenases [Energy production and conversion] | ||
pfam08031 | BBE | 2.0e-12 | 489 | 533 | 45 | + 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 | 2.0e-14 | 88 | 234 | 148 | + 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 | 2bvh_D | 0.0000000000004 | 100 | 535 | 51 | 457 | A Chain A, Structure Of Udp-Galactose 4-Epimerase Mutant |
PDB | 2bvh_C | 0.0000000000004 | 100 | 535 | 51 | 457 | A Chain A, Structure Of Udp-Galactose 4-Epimerase Mutant |
PDB | 2bvh_B | 0.0000000000004 | 100 | 535 | 51 | 457 | A Chain A, Structure Of Udp-Galactose 4-Epimerase Mutant |
PDB | 2bvh_A | 0.0000000000004 | 100 | 535 | 51 | 457 | A Chain A, Structure Of Udp-Galactose 4-Epimerase Mutant |
PDB | 2bvg_D | 0.0000000000004 | 100 | 535 | 51 | 457 | A Chain A, Structure Of Udp-Galactose 4-Epimerase Mutant |
Sequence Alignments (This image is cropped. Click for full image.) |
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