dbCAN-seq: a database of CAZyme sequence and annotation

You are browsing environment: FUNGIDB

help

CAZyme Information: AKAW_04363-t41_1-p1

You are here: Home > Sequence: AKAW_04363-t41_1-p1

Basic Information help

Species

Aspergillus luchuensis

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus luchuensis

CAZyme ID

AKAW_04363-t41_1-p1

CAZy Family

GH11

CAZyme Description

FAD linked oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
591		66848.50	6.3147

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	69	508	4.7e-75	0.982532751091703

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.98e-30	75	498	31	446	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	3.65e-28	76	209	1	135	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.
369658	BBE	6.46e-15	465	509	1	45	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	2.04e-12	68	223	59	220	cytokinin dehydrogenase
273751	FAD_lactone_ox	1.29e-04	59	225	1	162	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
5.13e-34	50	508	40	489
5.13e-34	50	508	40	489
6.99e-34	50	508	40	489
5.14e-29	43	508	24	482
1.01e-28	50	508	41	490

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
7.63e-35	45	508	15	459	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
1.93e-34	45	508	15	459	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
3.57e-34	45	508	15	459	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]
4.86e-34	45	508	15	459	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]
6.61e-34	45	508	15	459	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.10e-48	68	508	24	442	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
9.01e-38	50	512	8	447	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
5.64e-30	65	508	64	521	Berberine bridge enzyme-like 14 OS=Arabidopsis thaliana OX=3702 GN=At1g34575 PE=3 SV=1
1.24e-28	66	508	70	536	Berberine bridge enzyme-like 16 OS=Arabidopsis thaliana OX=3702 GN=At2g34810 PE=2 SV=1
1.38e-28	75	242	78	243	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000034	0.000000

TMHMM Annotations help

There is no transmembrane helices in AKAW_04363-t41_1-p1.