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CAZyme Information: OAG21338.1

You are here: Home > Sequence: OAG21338.1

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 Alternaria alternata
Lineage Ascomycota; Dothideomycetes; ; Pleosporaceae; Alternaria; Alternaria alternata
CAZyme ID OAG21338.1
CAZy Family GH3
CAZyme Description FAD-linked oxidase-like protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
569 KV441477|CGC5 63902.93 7.0663
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AalternataSRC1lrK2f 13577 N/A 111 13466
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in OAG21338.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 31 562 2.5e-152 0.9885057471264368

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
396238 FAD_binding_4 1.95e-29 82 221 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 1.18e-28 47 552 1 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
183043 PRK11230 1.15e-10 34 282 14 245
glycolate oxidase subunit GlcD; Provisional
178402 PLN02805 3.60e-10 81 266 133 309
D-lactate dehydrogenase [cytochrome]
273751 FAD_lactone_ox 4.76e-05 88 288 21 197
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
0.0 5 569 5 569
0.0 3 569 2 568
2.63e-287 2 564 4 568
1.73e-278 3 564 6 568
1.55e-239 3 560 6 563

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.33e-108 32 564 5 526
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]
9.94e-103 32 559 12 553
Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
1.40e-102 32 559 12 553
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum],1W1J_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum]
1.40e-102 32 559 12 553
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]
2.77e-102 32 559 12 553
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
2.01e-101 32 559 12 553
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
1.06e-96 30 554 7 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
2.20e-16 57 266 28 218
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
2.75e-14 45 285 11 240
Lactate dehydrogenase (NAD(+),ferredoxin) subunit LctD OS=Acetobacterium woodii (strain ATCC 29683 / DSM 1030 / JCM 2381 / KCTC 1655 / WB1) OX=931626 GN=lctD PE=1 SV=1
2.94e-14 27 286 14 261
Probable D-lactate dehydrogenase, mitochondrial OS=Mus musculus OX=10090 GN=Ldhd PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000053 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in OAG21338.1.