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CAZyme Information: HMPREF1541_02096-t46_1-p1

You are here: Home > Sequence: HMPREF1541_02096-t46_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 Cyphellophora europaea
Lineage Ascomycota; Eurotiomycetes; ; Cyphellophoraceae; Cyphellophora; Cyphellophora europaea
CAZyme ID HMPREF1541_02096-t46_1-p1
CAZy Family AA7
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
599 KB822718|CGC19 66489.28 6.5428
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CeuropaeaCBS101466 11153 1220924 59 11094
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in HMPREF1541_02096-t46_1-p1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 35 591 1e-137 0.9865900383141762

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 5.84e-31 86 225 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.
223354 GlcD 1.08e-28 51 582 1 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
183043 PRK11230 2.64e-11 73 270 43 232
glycolate oxidase subunit GlcD; Provisional
178402 PLN02805 8.98e-11 85 286 133 325
D-lactate dehydrogenase [cytochrome]
273751 FAD_lactone_ox 1.56e-04 86 335 15 240
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
1.79e-270 7 590 3 560
1.19e-263 9 591 4 560
1.03e-251 2 590 1 564
9.94e-245 2 590 1 564
7.19e-221 6 598 4 574

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.53e-100 36 590 5 522
Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1]
2.32e-94 36 589 12 553
Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
3.26e-94 36 589 12 553
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum]
6.44e-94 36 589 12 553
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum],1W1J_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum]
6.44e-94 36 589 12 553
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.65e-93 36 589 12 553
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
8.01e-80 34 584 7 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
1.84e-16 83 270 38 218
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
1.14e-15 46 283 33 261
Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
4.02e-15 56 268 12 214
Uncharacterized FAD-linked oxidoreductase Rv2280 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2280 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000062 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in HMPREF1541_02096-t46_1-p1.