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CAZyme Information: PITG_20764-t26_1-p1

You are here: Home > Sequence: PITG_20764-t26_1-p1

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 Phytophthora infestans
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora infestans
CAZyme ID PITG_20764-t26_1-p1
CAZy Family PL1
CAZyme Description conserved hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
505 54720.95 4.5693
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PinfestansT30-4 19344 403677 1547 17797
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 80 499 4.9e-71 0.980349344978166

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 4.04e-19 64 501 5 458
FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658 BBE 2.40e-16 455 500 2 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.
396238 FAD_binding_4 8.88e-10 86 210 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.
215242 PLN02441 6.81e-04 196 233 196 232
cytokinin dehydrogenase
273751 FAD_lactone_ox 0.001 85 264 14 200
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
3.62e-46 81 501 61 492
3.76e-46 111 499 108 491
3.76e-46 111 499 108 491
3.76e-46 111 499 108 491
3.76e-46 111 499 108 491

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.95e-45 81 499 38 476
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]
3.58e-44 81 499 38 476
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
7.50e-43 111 499 105 488
Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
8.07e-41 82 500 41 460
The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
1.11e-40 82 500 41 460
The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.38e-45 81 499 57 495
Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
9.36e-44 107 500 72 444
Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
1.31e-42 33 500 31 534
Berberine bridge enzyme-like 19 OS=Arabidopsis thaliana OX=3702 GN=At4g20830 PE=1 SV=2
1.36e-42 63 500 10 443
Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
3.86e-42 111 499 105 488
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

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000213 0.999762 CS pos: 22-23. Pr: 0.9736

TMHMM  Annotations      help

There is no transmembrane helices in PITG_20764-t26_1-p1.