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CAZyme Information: An01g14520-T-p1

You are here: Home > Sequence: An01g14520-T-p1

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 niger
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
CAZyme ID An01g14520-T-p1
CAZy Family AA3
CAZyme Description Has domain(s) with predicted UDP-N-acetylmuramate dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity and role in oxidation-reduction process
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
496 An01_A_niger_CBS_513_88|CGC1 53513.42 4.5774
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AnigerCBS513-88 14403 425011 346 14057
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 61 272 1.7e-68 0.4497816593886463

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 3.72e-30 67 493 28 456
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 1.08e-29 71 209 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 1.67e-12 71 245 134 312
D-lactate dehydrogenase [cytochrome]
369658 BBE 3.95e-12 450 493 1 44
Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
215242 PLN02441 1.21e-11 12 231 3 232
cytokinin dehydrogenase

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
2.05e-190 28 493 5 471
9.09e-177 33 496 10 474
2.59e-176 33 496 10 474
3.53e-176 33 496 19 483
1.05e-175 33 496 10 474

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
6.49e-63 63 496 53 495
Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]
1.08e-61 63 495 35 478
Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
2.10e-61 63 495 35 478
The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
7.95e-61 60 496 26 472
Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
1.27e-59 63 495 53 490
Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.90e-114 28 495 3 469
FAD-linked oxidoreductase sorD OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=sorD PE=3 SV=1
3.34e-62 63 496 53 495
Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1
9.90e-61 63 495 54 497
Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
6.73e-60 60 496 48 494
Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
6.51e-59 63 495 53 490
Chitooligosaccharide oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chitO PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as SP

Other SP_Sec_SPI CS Position
0.002275 0.997706 CS pos: 26-27. Pr: 0.9830

TMHMM  Annotations      help

There is no transmembrane helices in An01g14520-T-p1.