CAZyme Information: Afu6g12070-T-p1

Basic Information

• Species: Aspergillus fumigatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus fumigatus
• CAZyme ID: Afu6g12070-T-p1
• CAZy Family: GH76
• CAZyme Description: Flavoprotein amide oxidase (FAD)

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
493	Chr6_A_fumigatus_Af293|CGC23	53973.40	4.1909

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AfumigatusAf293	10130	330879	290	9840

• Gene Location: location=Chr6_A_fumigatus_Af293:3020103-3021926(+)

Full Sequence      

MQYIPFLISGLVPVALSKSLFEATSNTRIDGNDIAAIFGPVLTPEAHIFLPSDGDYDDNV
MARWSTFNDPSYVATVKPATETDVQAIVSTAASHNITFFATGGGHGVKLNFGNVQNAINI
ELSLLDFIDLDLDNEVVTIGPGVENAQLYDLLSSVGKETALTGERCVNTIGPTLGGGLGP
LYGIRGPQVDSLVSARLVTASGDVITVSRSENRDLFWAIRGAGANFGIVTSATYRIYDQT
NGGMAVSAQFAFAPAVNRSVFDLMESMNDEYPPGMSGGMILSYNHTTNEPSVQWNLLFMG
SNEDAQPWLDKIQALGPIDSSIRNVPWHRRDEPEVPYCERGQHYILYNLNLRRTDAATLQ
SYFDSFVDFSSKNPWFDCDLMYERQATDAALAVPLSERGVGPWRDSKINANFLVVTPSEE
YDEAADAFVRPFMDRFQAVMGFDTLHVYVNEALGDEGPASWYGEENLPRLVALKQQWDPE
NKFGAGAPIPLSL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	62	284	3e-45	0.48034934497816595

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.10e-12	74	483	34	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	7.63e-09	70	208	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.
369658	BBE	6.21e-06	447	490	1	45	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.
215242	PLN02441	1.56e-04	186	236	188	236	cytokinin dehydrogenase
273751	FAD_lactone_ox	0.005	78	241	21	183	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
AEO62186.1|AA7	2.18e-19	73	483	60	482
VBB87167.1|AA7	7.13e-19	50	483	39	488
AAS79317.1|AA7|1.1.3.-	9.62e-19	69	484	61	490
CAP69207.1|AA7	3.04e-18	50	483	39	488
CDP32688.1|AA7	3.04e-18	50	483	39	488

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	1.06e-21	42	483	10	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]
3HSU_A	2.53e-20	69	484	42	471	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	3.38e-20	69	484	42	471	The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
5K8E_A	7.86e-20	65	483	51	486	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]
6Y0R_AAA	3.27e-19	69	483	60	482	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q4WLW6|FMQD_ASPFU	0.0	1	493	1	497	FAD-linked oxidoreductase fmqD OS=Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100) OX=330879 GN=fmqD PE=1 SV=1
sp|G3XMD0|AZAL_ASPNA	1.99e-104	32	474	21	471	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|Q5BEJ5|AFOF_EMENI	2.02e-100	33	490	20	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|Q0CF74|AZPB3_ASPTN	2.85e-100	17	489	8	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|Q7SHH8|SRDI_NEUCR	1.16e-94	23	492	23	498	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

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.622832	0.377163

TMHMM  Annotations     

There is no transmembrane helices in Afu6g12070-T-p1.