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CAZyme Information: EAW22365.1

You are here: Home > Sequence: EAW22365.1

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 Aspergillus fischeri
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
CAZyme ID EAW22365.1
CAZy Family GH71|CBM24|CBM24
CAZyme Description sugar 1,4-lactone oxidase, putative
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
589 66749.81 6.7309
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AfischeriNRRL181 10668 331117 278 10390
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:2

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 38 214 1.1e-28 0.3864628820960699

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
273751 FAD_lactone_ox 2.22e-142 39 481 7 436
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.
397924 ALO 3.70e-106 206 488 1 259
D-arabinono-1,4-lactone oxidase. This domain is specific to D-arabinono-1,4-lactone oxidase EC:1.1.3.-, which is involved in the final step of the D-erythroascorbic acid biosynthesis pathway.
223354 GlcD 3.14e-45 46 480 31 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].
215258 PLN02465 6.35e-41 39 484 89 565
L-galactono-1,4-lactone dehydrogenase
396238 FAD_binding_4 2.55e-38 47 182 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.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.11e-12 53 396 170 522
9.69e-12 92 480 121 491
2.21e-11 58 230 73 256
3.51e-10 53 208 50 208
3.70e-10 47 209 61 226

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
9.26e-28 34 492 110 607
Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea]
4.52e-19 32 480 6 411
Alditol Oxidase from Streptomyces coelicolor A3(2): Native Enzyme [Streptomyces coelicolor A3(2)],2VFS_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Xylitol [Streptomyces coelicolor A3(2)],2VFT_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sorbitol [Streptomyces coelicolor A3(2)],2VFU_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Mannitol [Streptomyces coelicolor A3(2)],2VFV_A Alditol Oxidase from Streptomyces coelicolor A3(2): Complex with Sulphite [Streptomyces coelicolor A3(2)]
1.79e-14 59 487 44 464
Chain A, Decaprenyl-phosphoryl-beta-d-ribofuranose-2- Oxidoreductase [Mycolicibacterium smegmatis],4F4Q_A Crystal structure of M. smegmatis DprE1 in complex with FAD and covalently bound BTZ043 [Mycolicibacterium smegmatis MC2 155]
2.29e-13 92 487 13 399
Chain A, oxidoreductase DprE1 [Mycolicibacterium smegmatis],4G3U_A Chain A, oxidoreductase DprE1 [Mycolicibacterium smegmatis],4G3U_B Chain B, oxidoreductase DprE1 [Mycolicibacterium smegmatis]
1.28e-11 47 209 61 226
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]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.06e-202 29 531 33 548
Putative D-arabinono-1,4-lactone oxidase OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=alo-1 PE=3 SV=1
7.15e-125 34 481 13 514
D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1
6.17e-109 31 481 13 543
D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1
1.35e-107 35 481 18 542
D-arabinono-1,4-lactone oxidase OS=Debaryomyces hansenii (strain ATCC 36239 / CBS 767 / BCRC 21394 / JCM 1990 / NBRC 0083 / IGC 2968) OX=284592 GN=ALO1 PE=3 SV=2
6.84e-104 33 498 15 532
D-arabinono-1,4-lactone oxidase OS=Ashbya gossypii (strain ATCC 10895 / CBS 109.51 / FGSC 9923 / NRRL Y-1056) OX=284811 GN=ALO1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000066 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in EAW22365.1.