logo
sublogo
You are browsing environment: FUNGIDB
help

CAZyme Information: EKG15142.1

You are here: Home > Sequence: EKG15142.1

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 Macrophomina phaseolina
Lineage Ascomycota; Dothideomycetes; ; Botryosphaeriaceae; Macrophomina; Macrophomina phaseolina
CAZyme ID EKG15142.1
CAZy Family GH17
CAZyme Description FAD-linked oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
555 62113.90 6.8541
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_MphaseolinaMS6 14712 1126212 906 13806
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.38:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 6 550 2.6e-245 0.9904214559386973

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 3.26e-30 66 208 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 9.35e-28 37 541 7 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
397178 FAD-oxidase_C 4.36e-12 438 540 147 247
FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
183043 PRK11230 1.44e-08 25 553 25 483
glycolate oxidase subunit GlcD; Provisional
178402 PLN02805 3.74e-08 46 211 114 274
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 555 1 555
2.20e-278 6 555 7 557
6.81e-269 2 548 24 572
8.99e-269 6 548 28 572
9.30e-269 5 555 8 560

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.47e-270 5 555 8 560
Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8F_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8G_A STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8G_B STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8H_A Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum],1E8H_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum]
1.85e-269 5 555 8 560
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum]
2.62e-269 3 555 6 560
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
7.49e-269 5 555 8 560
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]
7.49e-269 5 555 8 560
Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHU_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHV_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHV_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHZ_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1AHZ_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],1VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],2VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],2VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.86e-268 5 555 8 560
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
1.47e-119 1 543 1 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
8.68e-16 35 268 13 217
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
6.29e-13 68 540 68 482
Probable D-lactate dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ldhd PE=1 SV=1
4.56e-11 68 540 68 505
Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000050 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in EKG15142.1.