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CAZyme Information: NEUDI_156576T0-p1

You are here: Home > Sequence: NEUDI_156576T0-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 Neurospora discreta
Lineage Ascomycota; Sordariomycetes; ; Sordariaceae; Neurospora; Neurospora discreta
CAZyme ID NEUDI_156576T0-p1
CAZy Family GH15|CBM20
CAZyme Description D-arabinono-1, 4-lactone oxidase
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
556 NdisFGSC8579_SC007|CGC6 62554.92 6.7824
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_NdiscretaFGSC8579 10345 510953 397 9948
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 42 238 1.9e-30 0.4388646288209607

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
273751 FAD_lactone_ox 3.61e-137 39 505 3 435
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 9.44e-114 210 513 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.
215258 PLN02465 6.19e-44 43 509 89 565
L-galactono-1,4-lactone dehydrogenase
396238 FAD_binding_4 5.24e-38 51 186 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 3.62e-37 40 505 21 450
FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
5.24e-10 51 225 164 349
9.76e-10 29 225 18 229
1.34e-09 51 213 63 228
2.32e-09 51 237 61 257
3.55e-09 51 228 135 321

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.23e-28 38 266 110 337
Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea]
1.14e-21 43 220 13 186
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)]
3.98e-13 23 269 21 278
Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2) [Zea mays],4ML8_B Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2) [Zea mays],4ML8_C Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2) [Zea mays],4ML8_D Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2) [Zea mays],4MLA_A Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2) [Zea mays],4MLA_B Structure of maize cytokinin oxidase/dehydrogenase 2 (ZmCKO2) [Zea mays]
1.06e-11 31 258 25 253
The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
1.86e-11 31 258 25 253
The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
0.0 1 556 1 556
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
4.47e-123 34 506 9 514
D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1
5.26e-104 31 506 10 543
D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1
5.87e-99 38 506 16 513
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
9.56e-99 32 506 6 509
D-arabinono-1,4-lactone oxidase OS=Candida glabrata (strain ATCC 2001 / CBS 138 / JCM 3761 / NBRC 0622 / NRRL Y-65) OX=284593 GN=ALO1 PE=3 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000055 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in NEUDI_156576T0-p1.