CAZyme Information: AN1035-T-p1

Basic Information

• Species: Aspergillus nidulans
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus nidulans
• CAZyme ID: AN1035-T-p1
• CAZy Family: AA7
• CAZyme Description: Putative FAD/FMN-dependent oxygenase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
481	ChrVIII_A_nidulans_FGSC_A4|CGC18	52261.93	4.4830

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnidulansFGSCA4	10988	227321	276	10712

• Gene Location: location=ChrVIII_A_nidulans_FGSC_A4:1731554-1733146(-)

Full Sequence      

MRFLLQSITLVAAARAASIDLESLFGPYVSPETEIAEVGDADFDEVVSPRWSEWRPPTWT
GAIKPQTEEDLQEIVRIAVANNVSFMATSGGHGTSLIYGTVKGLDINLANFNNVDIDLES
NTVTVGAGAKLGDITEPLYKAGKAIQTARGNSPCVGVIGATIGGGIGYETGLFGLGVDAL
VSVRIITATGELITANETCNSDLLWAIRGAGANFGIITAATFKMFDQPNNGDAVIGTFVY
NSSKSLGVFEYLSVLDNVLPPELGVQLSIGYDRTINETLLTVDIKHFAPWATFVDHWEHA
EALGPISRNVSNVTLVELYAGLDGPCQTGAYVSGGTVGLGRTDAATMQEVFDDMTAFYEQ
YPGYLGQSLFQRYANNNTLKTPAHTAVYPWRDTKMFWLHENIFLNPELEAPTNELLVSLR
EKLHATSGFPADQPHIYVNYAFGDEGPEAWWSKENLPKLSYLKRKWDPKGVFGKGTPIPR
F

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	65	249	1.5e-51	0.3951965065502183

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.22e-18	63	472	36	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	5.06e-18	63	196	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.
223882	MurB	2.09e-08	63	223	25	179	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].
273751	FAD_lactone_ox	6.27e-08	65	223	21	177	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.
237553	murB	2.90e-06	63	234	35	197	UDP-N-acetylmuramate dehydrogenase.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRC92907.1|AA7	8.87e-39	5	472	9	484
UNI23960.1|AA7	4.14e-30	56	472	45	463
QUC19098.1|AA7	1.40e-29	63	472	52	462
EGX49222.1|AA7|CBM1	3.65e-27	56	472	161	586
AEO62186.1|AA7	1.12e-26	11	472	9	482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	9.94e-28	56	230	58	233	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]
3HSU_A	8.67e-27	65	478	49	476	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	1.58e-26	65	478	49	476	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]
6Y0R_AAA	9.71e-25	65	472	67	482	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
2BVF_A	1.51e-23	70	286	50	263	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|Q5BEJ5|AFOF_EMENI	0.0	1	481	1	481	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	6.01e-264	1	478	2	480	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|G3XMD0|AZAL_ASPNA	6.10e-109	4	463	6	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|Q4WLW6|FMQD_ASPFU	4.89e-99	20	479	33	494	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|G3XMC1|AZAG_ASPNA	3.21e-95	14	462	16	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.002349	0.997619	CS pos: 16-17. Pr: 0.9476

TMHMM  Annotations     

There is no transmembrane helices in AN1035-T-p1.