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CAZyme Information: KFA50647.1

You are here: Home > Sequence: KFA50647.1

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 Stachybotrys chartarum
Lineage Ascomycota; Sordariomycetes; ; Stachybotryaceae; Stachybotrys; Stachybotrys chartarum
CAZyme ID KFA50647.1
CAZy Family GH13
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
495 KL651415|CGC3 52932.29 7.1556
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_SchartarumIBT40293 11453 1280524 0 11453
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:3

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 54 491 1.4e-91 0.9934497816593887

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 3.18e-28 37 494 2 459
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 1.13e-24 66 202 1 139
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.
369658 BBE 1.96e-13 447 491 2 44
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.
215242 PLN02441 8.17e-07 55 224 54 232
cytokinin dehydrogenase
273751 FAD_lactone_ox 0.003 72 223 21 171
sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.54e-164 6 494 3 492
8.75e-163 28 493 24 492
2.78e-162 27 493 24 490
3.52e-162 28 493 24 492
3.52e-162 28 493 24 492

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.34e-158 27 493 22 490
Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
5.22e-158 3 494 5 504
Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]
3.46e-151 32 493 9 478
The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
7.91e-150 32 493 9 478
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
2.10e-148 17 494 13 495
Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.87e-158 27 493 22 490
Chitooligosaccharide oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chitO PE=1 SV=1
4.21e-153 17 493 13 497
Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
1.08e-147 17 494 13 495
Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1
1.12e-139 24 494 21 492
FAD-linked oxidoreductase dpmaF OS=Metarhizium anisopliae OX=5530 GN=dpmaF PE=1 SV=1
6.37e-139 35 494 32 492
FAD-linked oxidoreductase subF OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=subF PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000285 0.999680 CS pos: 20-21. Pr: 0.9739

TMHMM  Annotations      help

There is no transmembrane helices in KFA50647.1.