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CAZyme Information: FOIG_11160-t36_1-p1

You are here: Home > Sequence: FOIG_11160-t36_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 Fusarium odoratissimum
Lineage Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
CAZyme ID FOIG_11160-t36_1-p1
CAZy Family GH36
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
466 51882.84 5.2281
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006 16975 1089451 341 16634
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 21 232 2.3e-57 0.45633187772925765

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 4.45e-29 6 374 4 389
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 5.67e-25 32 169 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.
273750 pln_FAD_oxido 4.00e-09 29 215 29 222
plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.
215242 PLN02441 5.77e-09 8 193 43 233
cytokinin dehydrogenase
273751 FAD_lactone_ox 3.89e-08 38 218 21 198
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
1.90e-22 30 200 18 188
6.32e-21 15 201 32 216
6.32e-21 15 201 32 216
2.07e-20 15 201 32 216
2.50e-19 21 229 154 352

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.65e-14 23 197 54 230
The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],2WDW_B The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],5AWV_A Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_B Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_C Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_D Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis]
2.76e-14 32 198 31 204
Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6]
9.00e-14 32 289 54 307
Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa]
2.82e-13 15 198 40 229
Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus],2IPI_B Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus],2IPI_C Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus],2IPI_D Crystal Structure of Aclacinomycin Oxidoreductase [Streptomyces galilaeus]
8.22e-13 23 198 53 226
Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
8.01e-52 9 454 16 442
FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
1.14e-51 15 454 19 441
FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
1.88e-36 8 449 12 434
FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
3.35e-35 8 449 12 434
FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
1.49e-18 6 234 9 238
Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000043 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in FOIG_11160-t36_1-p1.