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CAZyme Information: P174DRAFT_445350-t37_1-p1

You are here: Home > Sequence: P174DRAFT_445350-t37_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 Aspergillus novofumigatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus novofumigatus
CAZyme ID P174DRAFT_445350-t37_1-p1
CAZy Family GH31
CAZyme Description FAD binding domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
564 61313.01 6.8741
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AnovofumigatusIBT16806 11729 1392255 197 11532
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 135 323 9.6e-42 0.38427947598253276

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 3.20e-19 129 277 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 1.39e-14 109 542 12 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658 BBE 3.49e-08 505 541 1 37
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.
223882 MurB 3.07e-04 115 289 8 162
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.40e-41 34 554 517 1055
5.40e-41 34 554 517 1055
1.56e-13 137 309 56 217
1.63e-12 135 549 73 496
3.22e-12 129 308 20 188

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4.37e-60 33 554 44 564
Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
4.30e-39 35 552 48 586
Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
4.00e-16 137 541 53 452
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
9.42e-16 137 541 53 452
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]
2.21e-15 137 541 53 452
The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.13e-154 36 551 30 589
FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
3.06e-135 28 563 25 580
FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
1.60e-134 39 563 76 612
FAD-linked oxidoreductase cheF OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=cheF PE=2 SV=1
1.89e-118 12 457 10 422
FAD-linked oxidoreductase phmC OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=phmC PE=3 SV=2
2.54e-63 35 549 45 558
Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02478 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.000224 0.999760 CS pos: 23-24. Pr: 0.6957

TMHMM  Annotations      help

There is no transmembrane helices in P174DRAFT_445350-t37_1-p1.