dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: AKAW_10898-t41_1-p1

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Basic Information help

Species

Aspergillus luchuensis

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis

CAZyme ID

AKAW_10898-t41_1-p1

CAZy Family

GT4

CAZyme Description

sugar 1,4-lactone oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
578	DF126503\|CGC1	65107.92	6.3774

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AluchuensisIFO4308	11755	1033177	267	11488

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	28	223	2e-26	0.4366812227074236

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
273751	FAD_lactone_ox	3.80e-144	29	471	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	2.87e-108	196	477	1	258	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	1.32e-42	27	470	21	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215258	PLN02465	9.14e-40	29	482	89	573	L-galactono-1,4-lactone dehydrogenase
396238	FAD_binding_4	9.36e-39	37	172	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
3.39e-09	82	195	121	234
1.79e-08	37	195	62	223
2.40e-08	37	209	59	235
2.76e-08	37	216	164	354
7.30e-08	37	182	61	209

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
1.17e-24	29	246	115	331	Assembly intermediate of the plant mitochondrial complex I [Brassica oleracea]
7.89e-18	29	206	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)]
1.03e-09	49	473	44	460	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]
1.37e-09	37	209	37	213	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]
2.52e-09	37	182	61	209	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
1.34e-205	3	521	13	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
2.23e-120	20	471	9	514	D-arabinono-1,4-lactone oxidase OS=Yarrowia lipolytica (strain CLIB 122 / E 150) OX=284591 GN=ALO1 PE=3 SV=1
5.40e-107	25	471	17	543	D-arabinono-1,4-lactone oxidase OS=Candida albicans (strain SC5314 / ATCC MYA-2876) OX=237561 GN=ALO1 PE=1 SV=1
1.14e-105	29	471	21	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
3.29e-105	21	477	14	550	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

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000063	0.000000

TMHMM Annotations help

There is no transmembrane helices in AKAW_10898-t41_1-p1.