dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: An07g04390-T-p1

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Basic Information help

Species

Aspergillus niger

Lineage

Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger

CAZyme ID

An07g04390-T-p1

CAZy Family

GH16

CAZyme Description

Has domain(s) with predicted UDP-N-acetylmuramate dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity, oxidoreductase activity, acting on CH-OH group of donors activity

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
573	An07_A_niger_CBS_513_88\|CGC3	65019.50	7.1652

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.-:2

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA7	74	496	1.6e-73	0.9716157205240175

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	4.75e-28	75	486	31	446	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	8.49e-26	76	213	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.
215242	PLN02441	3.01e-13	67	223	58	220	cytokinin dehydrogenase
369658	BBE	5.32e-13	453	497	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.
273751	FAD_lactone_ox	1.50e-04	84	225	23	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
1.54e-25	50	496	40	489
1.54e-25	50	496	40	489
2.08e-25	50	496	40	489
1.20e-23	75	500	45	476
1.88e-21	50	496	41	490

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
6.55e-33	49	496	19	459	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
1.65e-32	49	496	19	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]
3.04e-32	49	496	19	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]
4.13e-32	49	496	19	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]
5.61e-32	49	496	19	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
8.19e-43	62	496	18	442	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
7.72e-33	50	496	8	443	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
1.32e-27	49	260	12	216	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
2.53e-26	76	288	79	288	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
2.97e-25	65	496	70	529	Berberine bridge enzyme-like 13 OS=Arabidopsis thaliana OX=3702 GN=At1g30760 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000013	0.000034

TMHMM Annotations help

There is no transmembrane helices in An07g04390-T-p1.