CAZyme Information: EAW19902.1

Basic Information

• Species: Aspergillus fischeri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fischeri
• CAZyme ID: EAW19902.1
• CAZy Family: GH28
• CAZyme Description: FAD binding domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
466		51255.09	5.6088

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfischeriNRRL181	10668	331117	278	10390

• Gene Location: location=DS027694:444903-446422(+)

Full Sequence      

MAFQQLRAQLDVHATVVFPGDQDWDDSVKRWSAIGFRRPGVVVLPTDVQGIARTVRYAKD
HKLDLAVQGGGHSSNTASSTDGGILLNLGKMNRVSVDTSTQTVTVQGGATWADVARETAK
YQLAVNGGTTSQVGVGGLTLRGGFGFLTPQHGVTLDTLLAAKVVTAEGIELQVSTEEHPD
LFWAIRGAGPNVAVVAEFTFQAYPQPNLVWSGLRIHPSSEVSKVVEALNQALVHPQGRAA
AQCILCLSPEDERTPSVTTIIFFNGSEEEGRRHFAQLLEVECIKDDIKMRPYSETLGIWD
RLAPPGDRKRELGIQMTLPPRLAFLSELMDKISDKLTKEPDLAKTDLEIDYLDPTQICRT
PITETAFPTRLNSLLHATLMLQWTDADKDEDFLSWGQSIQKMCENELTSQGHKLAHTVSN
YNGYTQEIKVAAADMFGVNAERLLHVKAKYDPANIFNKLNPLDRNL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	31	260	1.5e-67	0.5021834061135371

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.88e-36	37	457	30	451	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.29e-34	39	174	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.
273751	FAD_lactone_ox	5.37e-17	29	230	5	199	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.
215242	PLN02441	5.73e-15	39	187	65	223	cytokinin dehydrogenase
215258	PLN02465	1.37e-12	28	209	86	267	L-galactono-1,4-lactone dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QLI74064.1|AA7	4.31e-29	11	456	35	483
AAS79317.1|AA7|1.1.3.-	2.89e-27	39	209	62	234
ADI58761.1|AA7|1.1.3.-	7.80e-27	39	209	37	209
UQC87672.1|AA7	1.24e-24	14	228	45	259
AEO62186.1|AA7	1.63e-24	19	209	39	232

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	2.75e-52	1	456	1	448	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]
6FYG_A	8.58e-46	16	456	22	453	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]
6FYD_A	1.19e-45	16	456	22	453	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]
4XLO_A	4.41e-45	16	456	22	453	Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
3W8W_A	4.75e-45	16	456	26	457	The crystal structure of EncM [Streptomyces maritimus],3W8W_B The crystal structure of EncM [Streptomyces maritimus],3W8X_A The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8X_B The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8Z_A The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus],3W8Z_B The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A2V5HCN7|PYVE_ASPV1	1.40e-84	14	458	13	445	FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1
sp|P08159|HDNO_PAENI	7.28e-51	5	456	4	447	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|Q54H55|Y8969_DICDI	9.31e-44	12	456	20	441	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|Q7SHH8|SRDI_NEUCR	1.50e-36	16	462	51	495	FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1
sp|P9WEY2|DPMAF_METAN	1.87e-31	11	456	35	483	FAD-linked oxidoreductase dpmaF OS=Metarhizium anisopliae OX=5530 GN=dpmaF PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000047	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EAW19902.1.