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CAZyme Information: PWY90671.1

You are here: Home > Sequence: PWY90671.1

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 Aspergillus heteromorphus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus heteromorphus
CAZyme ID PWY90671.1
CAZy Family GT3
CAZyme Description FAD-binding domain-containing protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
495 MSFL01000002|CGC3 53826.39 4.9966
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AheteromorphusCBS117.55 11436 1448321 306 11130
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 56 486 3.4e-55 0.9737991266375546

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 5.58e-17 67 329 35 299
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 6.59e-11 64 203 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.
178402 PLN02805 2.60e-04 64 230 134 303
D-lactate dehydrogenase [cytochrome]
215242 PLN02441 3.73e-04 50 226 51 233
cytokinin dehydrogenase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
6.68e-27 18 486 15 477
1.13e-19 40 233 24 215
1.13e-19 40 233 24 215
3.64e-19 40 233 24 215
7.80e-15 6 233 32 261

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.31e-23 25 228 7 205
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]
2.37e-23 25 228 7 205
The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
2.37e-23 25 228 7 205
The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
4.30e-23 25 228 7 205
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]
4.30e-23 25 228 7 205
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.82e-162 24 494 5 476
FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
7.08e-122 27 494 44 513
FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
1.29e-84 21 491 35 513
FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
1.60e-70 23 494 40 524
FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
1.78e-62 6 495 8 500
Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
0.999933 0.000097

TMHMM  Annotations      help

There is no transmembrane helices in PWY90671.1.