CAZyme Information: P170DRAFT_358662-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_358662-t37_1-p1
• CAZy Family: AA8|AA3
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
559		61411.12	4.6683

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000004:2286591-2288371(-)

Full Sequence      

MITITSILSILLFTPFFTSTPPKCRCRPGDTCWPSLETWSQFNDSISGRLVATIPLGAPC
HGSNFDGSQCARLRDEWTSPKIHYESSSSVMAPYFANGSCDPFHAPGTPCTLDNYVVYAV
NVSTPDHVTKTLQFVAKHNIRLVVRNTGHDYLGKSTGAGALGLWMHHLTDIQIKDYRDPW
YAGKAITVGAGVMAVEAYWAADARGLQVVGGECPTVGIAGGYTQGGGHSALSSRHGLAAD
QVLSWEVVTADGELVTATREHHSDLYWALSGGGGGTYGVVWSMTAKAYPDTPVSGLSLTF
SREGIDADLFHYAASLFYETLLDLVDAGAMCTWGVANELFRIDPLTAPDIPVEELLHLIE
PFTDDLEDLGIAYNMSARQFPGFLAQYQSMMPEVPVGTQQIGGWLVPRDVVQDSSEEFSA
AWRRIVEDGAFIIGVGLNVSKAVVGDVDNAVLPAWRDALIHTAILTTWERDDKEKMRELQ
RKMTDEYVPELSRLAPDSGAYMNEADFRQPDFQKAFYGENYNRLREIKKKYDPNDLFFAP
TAVGSDEWTVSDEGRLCRV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	120	305	1e-46	0.39082969432314413

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.28e-23	120	258	5	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	4.63e-20	120	537	36	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	2.47e-15	500	544	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	1.25e-04	164	289	59	180	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.
171497	PRK12436	0.005	126	260	47	169	UDP-N-acetylmuramate dehydrogenase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	2.03e-65	19	558	495	1065
QKD57322.1|CBM91|GH43_11	2.03e-65	19	558	495	1065
UJO23499.1|AA7	5.61e-19	109	543	54	483
RDX44700.1|AA7|1.1.3.-	1.44e-16	136	304	89	250
SAM83140.1|AA7	2.13e-16	79	543	56	539

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	3.68e-139	22	558	26	573	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6F74_A	1.42e-71	22	558	28	597	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
3RJ8_A	2.37e-19	115	543	35	469	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]
5I1V_A	4.77e-18	205	537	116	491	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]
4PVK_A	1.98e-17	117	306	54	244	Phl p 4 I153V N158H variant, a glucose oxidase [Phleum pratense],4PWC_A Phl p 4 I153V N158H variant, a glucose oxidase, 3.5 M NaBr soak [Phleum pratense]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A1CFM2|PATO_ASPCL	3.44e-187	9	559	14	568	FAD-linked oxidoreductase patO OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patO PE=1 SV=1
sp|A0A0E0RTV6|ZEB1_GIBZE	1.29e-177	8	558	9	562	FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2
sp|A0A075TR33|PATO_PENEN	6.35e-177	7	558	14	566	FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1
sp|G0R6T3|SORD_HYPJQ	5.01e-169	23	559	38	573	FAD-linked oxidoreductase sor8 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=sor8 PE=3 SV=1
sp|A0A0C6E5D0|BET5_NEOBT	8.53e-143	23	559	31	586	FAD-linked oxidoreductase orf1 OS=Neocamarosporium betae OX=1979465 GN=orf1 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.233740	0.766246	CS pos: 19-20. Pr: 0.6826

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_358662-t37_1-p1.