CAZyme Information: AO090009000091-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090009000091-T-p1
• CAZy Family: GH105
• CAZyme Description: Has domain(s) with predicted UDP-N-acetylmuramate dehydrogenase activity, flavin adenine dinucleotide binding, oxidoreductase activity and role in oxidation-reduction process

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
553	Chr1_A_oryzae_RIB40|CGC15	62103.44	5.9741

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AoryzaeRIB40	12364	510516	274	12090

• Gene Location: location=Chr1_A_oryzae_RIB40:259855-261516(+)

Full Sequence      

MPNADIYKDLKDKKVLGTQIPVYKSGDLEYEVSVDVANLLYRFSRPTCVVKPELPVHVEE
VVKYAYENKTPITVKNGGHSYAGLSTTNDGILLDLSRMNDVYLQHKSEPPTITMQGGALW
AHAYRQLVIEKVNKLVVNGGRCPTVGVSGFVLGGGLGPFTRKFGMGCDSLLEATLVTGKG
DLVTVRKDDLDPEKRKLFWALCGAGANNFGAVITMKMSLHELQEDKVVAGRYTWYPSTDE
REEGFMEAMNSFYAANWSNSMTIDTSWFCDLKDGKGDLAVRFLTYYDGKKQEFQEEIDRN
LRGDAGSDIHKIKNSLADNLKRRSIAEDSSRFLHETLVSQWSEETKKAIPSNKAYSIYAS
FVFGTGSDYTGITKSIRDHMKNFKKEFRGESALLQVTFIHTGQQATRIGANETAFPWRDA
SRIAYIMLQWDEKWLGEEMVEFCKNFKENLMQFSIDGKAGFLNFPDRELCVTEDHHQAYY
GPNSDAIREIKQTWDPKGIFQFAPKNERDESIATDIVPILQAALSIEEIVSASLPHLNPL
MTLISQLSAGNLS

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	44	502	2.1e-63	0.962882096069869

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	7.96e-32	46	186	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	3.30e-28	45	500	31	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	2.97e-06	461	503	2	41	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	1.19e-05	58	193	27	156	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	3.72e-05	32	214	53	232	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAE7214923.1|AA7	9.77e-29	19	500	37	483
QRC92907.1|AA7	1.96e-24	19	501	37	485
QLI74064.1|AA7	1.89e-20	19	519	37	502
EGX49222.1|AA7|CBM1	6.01e-18	20	500	139	586
UNI23960.1|AA7	2.81e-16	46	500	48	463

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	7.74e-24	45	240	38	222	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]
3FW9_A	4.40e-23	26	500	23	485	Structure of berberine bridge enzyme in complex with (S)-scoulerine [Eschscholzia californica]
3GSY_A	5.09e-23	26	500	29	491	Structure of berberine bridge enzyme in complex with dehydroscoulerine [Eschscholzia californica]
3D2D_A	5.61e-23	26	500	48	510	Structure of berberine bridge enzyme in complex with (S)-reticuline [Eschscholzia californica],3D2H_A Structure of berberine bridge enzyme from Eschscholzia californica, monoclinic crystal form [Eschscholzia californica],3D2J_A Structure of berberine bridge enzyme from Eschscholzia californica, tetragonal crystal form [Eschscholzia californica]
4EC3_A	6.80e-23	26	500	29	491	Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline [Eschscholzia californica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q796Y5|YGAK_BACSU	3.46e-24	62	502	49	438	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
sp|P08159|HDNO_PAENI	3.95e-23	45	240	37	221	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|P30986|RETO_ESCCA	2.89e-22	26	500	48	510	Reticuline oxidase OS=Eschscholzia californica OX=3467 GN=BBE1 PE=1 SV=1
sp|O06997|YVDP_BACSU	1.23e-21	21	502	16	439	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
sp|E9F5F1|SUBF_METRA	4.52e-20	20	519	38	502	FAD-linked oxidoreductase subF OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=subF PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000044	0.000000

TMHMM  Annotations     

There is no transmembrane helices in AO090009000091-T-p1.