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CAZyme Information: XP_001912294.1

You are here: Home > Sequence: XP_001912294.1

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 Podospora anserina
Lineage Ascomycota; Sordariomycetes; ; Podosporaceae; Podospora; Podospora anserina
CAZyme ID XP_001912294.1
CAZy Family GT2
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:B2A9M6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
475 53833.63 6.6126
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_PanserinaSmat 10888 515849 370 10518
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in XP_001912294.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 2 443 3.1e-113 0.8160919540229885

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 4.78e-29 3 136 7 139
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 3.52e-22 3 429 38 416
FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402 PLN02805 7.70e-13 3 188 140 318
D-lactate dehydrogenase [cytochrome]
183043 PRK11230 1.23e-08 3 181 62 232
glycolate oxidase subunit GlcD; Provisional

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 3 475 92 547
0.0 3 472 92 544
2.08e-222 2 472 90 541
9.88e-204 3 475 91 544
7.11e-194 3 472 88 538

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.65e-77 2 475 59 503
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]
5.11e-72 2 472 76 532
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]
7.16e-72 2 472 76 532
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]
1.00e-71 2 472 76 532
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]
1.40e-71 2 472 76 532
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
1.01e-70 2 472 76 532
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
2.30e-63 5 427 66 474
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
1.86e-15 2 181 46 218
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
8.55e-11 3 188 152 330
D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1
5.33e-10 3 191 72 254
Probable D-lactate dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ldhd PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000074 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in XP_001912294.1.