CAZyme Information: AO090010000586-T-p1

Basic Information

• Species: Aspergillus oryzae
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus oryzae
• CAZyme ID: AO090010000586-T-p1
• CAZy Family: GH13|GH13
• CAZyme Description: Ortholog(s) have role in asperfuranone biosynthetic process, fumiquinazoline C biosynthetic process and extracellular region, fungal-type cell wall localization

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
507	Chr8_A_oryzae_RIB40|CGC1	55474.91	5.9818

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=Chr8_A_oryzae_RIB40:1850832-1852578(-)

Full Sequence      

MLRLKMEVVAALAAWAIASACENLPIANHWIRGLCPRSNDVKDLGIKLSPAAKVYFPGSE
EFEVASTRWSVLEAPKVNIVVVPGTENDVVETVKFANEKDLPFLAYNGAHGAITTLGKMD
HGIEIFLDQLNTIDIAKDGKTVKIGGGTKSKAVIDELWAAGKQTVSGTCECVSFLGPALG
GGHGWLQGHHGLVADQFISMNVVLADGSLKVLDKKSDLWWAMNGAGHNFGIVTSVTTKLY
DIVHYDWAIETLTFSGDKVEAVYQTANDHLLRNGTQPEGVINWSYWLNNPNADPENPVIL
FYIIQEGVKTVDSAYTKPFHDIGPLSTEPKGGSYTDLAEWTGISLSAPPCQKAGLVNPRF
PNYLEEYNVPAQKKAYEIFANAIRGSSAFNNSIFMFEGYSMQGVKAIDSKSSAFAFRGEN
ILSAPLITYAPAGPELDEKAAQLGNELRQVLHKASGRPEVRAYVNYAYGDESPQQWYGSE
KWRQDRLQALKKKYDPTGKFSFFAPVA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	74	268	2.8e-41	0.425764192139738

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	5.83e-21	79	213	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	1.91e-19	79	242	34	206	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	7.70e-06	462	502	1	40	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	0.002	83	236	21	175	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	1.85e-17	44	241	29	231
CEI70304.1|AA7	2.45e-17	58	500	42	482
CEF87481.1|AA7	7.76e-17	58	500	42	482
CZS85584.1|AA7	7.76e-17	58	500	42	482
ESU17750.1|AA7|1.1.3.-	7.76e-17	58	500	42	482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	5.07e-21	44	242	6	205	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]
6EO4_A	1.84e-20	52	502	23	464	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	3.29e-20	52	502	23	464	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6Y0R_AAA	2.68e-18	58	500	42	482	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
6FYG_A	9.97e-18	53	500	21	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6HLP5|CHYH_PENRW	2.84e-257	4	507	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	1.54e-215	6	507	3	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	3.81e-84	42	507	48	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	5.00e-72	25	506	24	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	8.27e-70	43	506	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
0.012126	0.987835	CS pos: 20-21. Pr: 0.9121

TMHMM  Annotations     

There is no transmembrane helices in AO090010000586-T-p1.