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CAZyme Information: KIW90104.1

You are here: Home > Sequence: KIW90104.1

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 Cladophialophora bantiana
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Cladophialophora; Cladophialophora bantiana
CAZyme ID KIW90104.1
CAZy Family GH1
CAZyme Description hypothetical protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
477 KN846994|CGC3 52410.52 6.9827
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CbantianaCBS173.52 12817 1442370 55 12762
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 48 251 1.5e-56 0.44541484716157204

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 2.27e-22 47 216 29 205
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 2.38e-22 50 186 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.
215242 PLN02441 2.21e-11 49 208 64 232
cytokinin dehydrogenase
215258 PLN02465 5.22e-05 39 216 87 262
L-galactono-1,4-lactone dehydrogenase
273751 FAD_lactone_ox 5.84e-05 41 216 7 180
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
6.23e-19 25 215 40 230
1.07e-16 48 212 46 212
9.31e-16 50 216 90 257
1.43e-15 48 219 46 219
2.04e-15 18 215 35 230

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.02e-20 58 276 53 295
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]
1.84e-20 58 276 53 295
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]
1.84e-20 58 276 53 295
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]
3.31e-20 58 276 53 295
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]
3.31e-20 58 276 53 295
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
1.96e-66 40 469 69 517
FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
2.01e-61 28 470 23 477
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
2.17e-58 23 469 55 513
FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
1.41e-50 5 469 23 507
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
1.41e-50 5 469 23 507
FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000046 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KIW90104.1.