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CAZyme Information: PHYSODRAFT_474098-t26_1-p1

You are here: Home > Sequence: PHYSODRAFT_474098-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 sojae
Lineage Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
CAZyme ID PHYSODRAFT_474098-t26_1-p1
CAZy Family GH5
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
507 54527.53 7.7243
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PsojaeP6497 28142 1094619 1653 26489
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 57 498 1.1e-54 0.982532751091703

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 1.22e-21 50 497 11 451
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 9.18e-20 68 205 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 1.08e-07 460 504 5 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.
273751 FAD_lactone_ox 8.30e-06 60 232 7 177
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.
215242 PLN02441 0.003 10 218 12 223
cytokinin dehydrogenase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.39e-314 1 507 2 505
2.27e-275 3 506 4 535
1.09e-93 37 504 27 492
1.03e-85 34 504 30 497
4.04e-85 34 504 30 497

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.88e-86 34 504 10 477
Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1],6YJI_B Chain B, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]
2.29e-51 33 496 8 470
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]
6.55e-51 32 503 1 469
Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
4.38e-50 33 496 8 470
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
3.61e-46 37 503 30 492
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
3.77e-51 25 503 16 491
Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
1.09e-50 33 496 27 489
Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
1.86e-45 37 503 30 492
Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1
1.15e-43 34 503 27 488
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
1.37e-41 37 507 32 493
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
0.445402 0.554598 CS pos: 27-28. Pr: 0.4390

TMHMM  Annotations      help

There is no transmembrane helices in PHYSODRAFT_474098-t26_1-p1.