CAZyme Information: P170DRAFT_407440-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_407440-t37_1-p1
• CAZy Family: GH16
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
500		54429.00	4.6805

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=MSFO01000004:416779-418582(+)

Full Sequence      

MRLQVVTAIAAWAVTSACQSLPVTRNLWSRDADYKELSEKLSTSAKVYYPGSDEFKKAST
RWSNLELPTVNIVVVPSTENDVVETVKFANKKELPFLAYNGAHGAITTLGKMTSGIEIYL
DQLSGVDVAEDGKTVTIAGGTKSKLVTDTLWEAGKQTVTGTCECVSYLGPALGGGHGWLQ
GHHGLVADQFESMNIVLSNGTLATLDSSSELWWAVKGAGHNFGIVTSVTSKVFDIEHKDW
AISTITFSGDKVEQVYEAANKYLLKNGTQPAGVINWSYWLNNPDADASNPVIIMYIIQEG
VKEVDSAYTAPFEEIGPISTDPQSGTYTDLAAWTNIALDSVPCQKSGLINPRFPNYLETY
NVAAQKQAYQVFADAVRGSSAFNGSIFMFEGYSMEGVKAIDAKSTAFAYRDENILSAPLI
TYKPDGAELDEKAAKLGNQLRQILQDASGTADVRAYVNYAYGDEGSEGWYGSESWRQSRL
QSLKKKYDPSGMFSFYAPIA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	60	495	1e-44	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.21e-18	72	206	3	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	3.91e-16	72	493	34	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	1.68e-05	76	236	21	185	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.
369658	BBE	2.97e-05	455	499	1	44	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI74064.1|AA7	1.89e-17	73	493	66	483
QRC92907.1|AA7	2.36e-17	37	234	29	231
QGI84728.1|AA7	7.55e-17	1	493	1	485
CCT71747.1|AA7	7.55e-17	1	493	1	485
QGI98385.1|AA7	7.55e-17	1	493	1	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	1.25e-17	36	249	5	225	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
6Y0R_AAA	1.93e-17	35	493	24	482	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
5K8E_A	4.46e-15	59	233	43	228	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]
6YJO_A	1.85e-13	64	233	62	235	Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]
6YJI_A	3.08e-13	68	493	42	469	Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1],6YJI_B Chain B, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6HLP5|CHYH_PENRW	6.87e-289	1	500	1	500	FAD-linked oxidoreductase chyH OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=chyH PE=3 SV=1
sp|I1S3L1|CHRY5_GIBZE	6.87e-246	1	500	1	506	FAD-linked oxidoreductase chry5 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chry5 PE=3 SV=1
sp|G4N287|OXR2_MAGO7	8.65e-84	22	500	35	520	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|G9N4A4|VIRI_HYPVG	5.02e-79	36	499	47	507	FAD-linked oxidoreductase virI OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virI PE=3 SV=1
sp|A0A1J0KJK5|IACH_PESFW	7.42e-79	36	499	48	507	FAD-linked oxidoreductase iacH OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=iacH PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000619	0.999408	CS pos: 17-18. Pr: 0.9705

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_407440-t37_1-p1.