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CAZyme Information: KAB8199951.1

You are here: Home > Sequence: KAB8199951.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Aspergillus parasiticus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus parasiticus
CAZyme ID KAB8199951.1
CAZy Family AA3
CAZyme Description chanoclavine-I synthase oxidoreductase protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
605 66498.11 6.3026
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AparasiticusCBS117618 14005 N/A 253 13752
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 127 316 4.9e-51 0.388646288209607

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 2.01e-19 127 270 5 139
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 oxidizes 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.
223354 GlcD 4.94e-11 121 368 30 276
FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242 PLN02441 3.87e-08 131 280 73 220
cytokinin dehydrogenase
369658 BBE 3.91e-06 519 562 1 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
3.31e-40 25 567 499 1055
3.31e-40 25 567 499 1055
3.49e-18 131 301 56 216
2.17e-17 121 555 58 484
9.01e-17 121 300 130 302

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.80e-64 6 573 9 573
Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
5.70e-47 9 574 7 598
Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
7.03e-20 131 300 56 216
Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
7.03e-20 131 300 56 216
Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
4.18e-17 123 301 53 224
Phl p 4 I153V variant, a glucose oxidase [Phleum pratense],4PWB_A Phl p 4 I153V variant, a glucose oxidase, pressurized with Xenon [Phleum pratense]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.32e-217 5 584 12 600
FAD-linked oxidoreductase easE OS=Arthroderma otae (strain ATCC MYA-4605 / CBS 113480) OX=554155 GN=easE PE=3 SV=1
3.38e-210 1 601 1 605
FAD-linked oxidoreductase easE OS=Epichloe festucae var. lolii OX=73839 GN=easE PE=2 SV=1
1.86e-209 4 569 3 580
FAD-linked oxidoreductase easE OS=Trichophyton verrucosum (strain HKI 0517) OX=663202 GN=easE PE=3 SV=1
6.58e-206 7 582 9 609
FAD-linked oxidoreductase ifgC OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=ifgC PE=3 SV=1
1.77e-189 5 573 8 573
FAD-linked oxidoreductase penH OS=Penicillium thymicola OX=293382 GN=penH PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000216 0.999750 CS pos: 21-22. Pr: 0.9815

TMHMM  Annotations      help

There is no transmembrane helices in KAB8199951.1.