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CAZyme Information: KEF53978.1

You are here: Home > Sequence: KEF53978.1

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 Exophiala aquamarina
Lineage Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala aquamarina
CAZyme ID KEF53978.1
CAZy Family CE4
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A072P3W6]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
525 AMGV01000011|CGC3 57735.13 6.9534
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_EaquamarinaCBS119918 13118 1182545 0 13118
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in KEF53978.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 25 511 1.8e-114 0.9099616858237548

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 4.39e-28 43 272 1 222
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 2.05e-27 74 213 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.
183043 PRK11230 2.60e-10 36 258 17 232
glycolate oxidase subunit GlcD; Provisional
178402 PLN02805 2.29e-08 40 272 98 323
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
9.29e-148 1 508 2 505
1.64e-144 4 508 10 520
3.83e-144 4 508 10 519
2.03e-141 4 510 7 518
9.48e-141 4 508 10 520

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
5.37e-80 28 504 5 474
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]
1.34e-73 27 516 7 487
p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVE_B p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVF_A p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida]
1.37e-73 27 516 8 488
Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DII_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_A Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida]
1.57e-68 21 510 5 512
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
2.20e-68 25 510 9 512
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.05e-73 27 516 8 488
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
8.39e-67 25 510 9 512
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
1.79e-19 74 271 41 231
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
4.07e-18 45 290 9 249
Uncharacterized FAD-linked oxidoreductase MT2338 OS=Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh) OX=83331 GN=MT2338 PE=3 SV=1
4.07e-18 45 290 9 249
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
1.000078 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in KEF53978.1.