CAZyme Information: ASPWEDRAFT_45261-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_45261-t33_1-p1
• CAZy Family: GH76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
595		66526.27	6.5117

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AwentiiDTO134E9	12659	1073089	224	12435

• Gene Location: location=KV878216:1319012-1320799(+)

Full Sequence      

MDELIRNLKSRRIAVYTAGELEYERSVANANLLFRYARPDCVVQPDSAWQIQKIVQEVKK
VNEAKSQGISIVVKNGGHSYAGFSTSDRGSISLDLVKMNHVEIDKESMTATIEGGAVWAH
AYRQLVNNHMDGYVINGGRCPSVGVSGFILGGGLSPFTRTFGMGCDGLKEATIVLADGRL
ITVGENDDATTNEGKLFWALRGAGGGNFGVVVEVKLSIYRLREIEKPSDDGTGVISGRYT
WSPKPSEKDMTEFMETMKKFYITPWPNSMTIDSTWICRLGYKDGELEVRFPVYFNGIKED
FDQIINEHIGEKHHLSKKLTRRCWQDKSTRFLHENLVSQWSEETQKALPSNASYRIFTSL
CFKADQRDDEGNNIFVRITETLRKEMAAFRQKFVGEEGTLQVTFIHAGGKATGPASNATA
FPWREAVYHAYIQMEWTDKWLELDMRGFCQRLKEELKPFSIEKGAAFINFPDGDLPPGQH
ESVYYGNNRHDLQRVKQIWDKDNFFKWKQGVGLPPTSQTPAATAGKKDDDPAAPQGDSAL
DSQVLTDKLAKEQWEKFDPSTALELAASLPFFPLGWALIPGLVAGLKSARLAGGE

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	37	509	6.5e-60	0.9672489082969432

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	5.84e-31	39	184	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	4.35e-24	37	238	30	218	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	4.27e-11	466	512	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	8.54e-09	37	228	13	191	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.
178402	PLN02805	4.60e-04	39	228	134	311	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEO63154.1|AA7	2.23e-26	8	511	32	489
QRW27390.1|AA7	5.48e-26	14	513	42	492
CAE7214923.1|AA7	2.50e-24	8	512	33	490
QLI74064.1|AA7	1.71e-22	8	511	33	489
QGI84728.1|AA7	2.77e-22	8	511	34	491

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I1V_A	1.67e-25	31	506	17	492	Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6]
6JQH_A	8.30e-24	15	515	25	516	Chain A, MaDA [Morus alba],6JQH_B Chain B, MaDA [Morus alba]
3VTE_A	1.12e-23	38	515	53	515	Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa]
2Y08_A	1.60e-23	19	515	40	529	Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y08_B Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y3R_A Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_B Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_C Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_D Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3S_A Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y3S_B Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y4G_A Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9],2Y4G_B Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9]
6EO5_A	3.65e-23	19	513	29	470	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q796Y5|YGAK_BACSU	5.51e-25	15	511	10	442	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
sp|Q9SVG7|BBE17_ARATH	5.86e-25	64	517	95	526	Berberine bridge enzyme-like 17 OS=Arabidopsis thaliana OX=3702 GN=At4g20800 PE=2 SV=1
sp|Q9SVG3|BBE21_ARATH	2.01e-24	38	511	85	532	Berberine bridge enzyme-like 21 OS=Arabidopsis thaliana OX=3702 GN=At4g20840 PE=2 SV=1
sp|Q9FZC6|FOX3_ARATH	4.46e-24	64	511	96	521	Berberine bridge enzyme-like 5 OS=Arabidopsis thaliana OX=3702 GN=FOX3 PE=3 SV=1
sp|Q9FZC5|FOX2_ARATH	4.55e-24	64	511	96	524	Berberine bridge enzyme-like 4 OS=Arabidopsis thaliana OX=3702 GN=FOX2 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000061	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPWEDRAFT_45261-t33_1-p1.