CAZyme Information: ASPNIDRAFT2_1169434-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ASPNIDRAFT2_1169434-t41_1-p1
• CAZy Family: GH7
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
489		52766.80	4.1478

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerATCC1015	11910	380704	6	11904

• Gene Location: location=ACJE01000001.1:452350-454070(-)

Full Sequence      

MFRTILLCSLGLTTLSSAATHNITSIFSSSLSPGAQIFLPSDTNYTEDVTQRWTTYDAPT
YIGAIKPATVKDIQNIVTLAASNKIPFLATAGGHGATITYVNCTNGIEIDISNFNTVSID
ASNNTMTVGGAVRFEDIIPPLYEAGKELPTGTAPCVGLVGATIGGGIGNLQGLHGLILDS
LLSVELVTPSGDVLTVSTSENADLFWAIRGAGANFGIITSATYKIYNATNNGLAMSANYL
FPASENRSVWEIFQSFDETLPPELSLTAYSGFNQTTQEMELIVNAIYYGPKEEGVSYLTN
FAALNATETNLMMVAWPNVTSSMAFGADGDACTTGSYLNTWGLGLAETNIDTYTTFFNEL
QAFSQAHPDYSGIFVVDRYSSAAAAAVPANSTSYGYGYRNINSHLLFENSYPSDNSTLDN
AVNSFMRSIRSQFQRTSGFSEMEIYLNYAHGDEGADVWYSPQHLPKLSQLKSKWDPDELF
SFNYPVPLP

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	65	483	2.9e-61	0.9519650655021834

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.51e-26	38	295	5	283	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	4.36e-25	65	197	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.
273751	FAD_lactone_ox	1.08e-10	51	225	5	178	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	7.54e-07	65	221	69	234	cytokinin dehydrogenase
273750	pln_FAD_oxido	9.80e-06	67	225	38	208	plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	3.14e-41	67	480	69	484
AEO62186.1|AA7	9.35e-34	67	482	65	484
ANF89368.1|AA7	8.20e-30	66	482	66	488
AEO58513.1|AA7|1.1.3.-	8.20e-30	66	482	66	488
CAP69207.1|AA7	1.12e-29	67	482	70	490

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	2.83e-31	66	482	66	488	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]
6EO4_A	3.75e-30	67	488	54	470	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	1.74e-29	67	488	54	470	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6YJO_A	8.89e-25	67	480	75	495	Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]
2BVF_A	4.88e-24	72	234	50	211	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G3XMD0|AZAL_ASPNA	0.0	1	472	1	472	FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2
sp|G3XMC1|AZAG_ASPNA	9.57e-132	17	470	17	468	FAD-linked oxidoreductase azaG OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaG PE=2 SV=1
sp|Q0CF74|AZPB3_ASPTN	1.04e-111	22	486	26	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|Q5BEJ5|AFOF_EMENI	4.64e-110	6	487	4	479	FAD-linked oxidoreductase afoF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=afoF PE=1 SV=1
sp|Q4WLW6|FMQD_ASPFU	3.30e-105	21	488	32	495	FAD-linked oxidoreductase fmqD OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fmqD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000257	0.999759	CS pos: 18-19. Pr: 0.9767

TMHMM  Annotations     

There is no transmembrane helices in ASPNIDRAFT2_1169434-t41_1-p1.