CAZyme Information: KAF7629516.1

Basic Information

• Species: Aspergillus flavus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus flavus
• CAZyme ID: KAF7629516.1
• CAZy Family: GT20
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
511		56140.81	7.4303

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AflavusNRRL3357	14313	332952	0	14313

• Gene Location: location=AAIH03000068:505470-507063(-)

Full Sequence      

MVMLYRCRYKIGRSTGGAAARGHIYYSSGFLLNVQLAYLTSPFRYMFFKPSRLTSTSTAE
WKMDQFFKFLAVNPRIKYARPTWPDFGGWRAGFVVDEDTIPAVIVRPRFAEDVAALVSVL
ATNNVPFSVRVGGHDMFGRSQIHDAVTIDLREIAYVDIDHTGHTARLGGGILVAGLIKEL
EKDNLVTPHGVIPGVGYVGWATHGGYGLLSTQYGLGVDQILDAQVVDCEGRIRHADKDML
KAIRGAGGLLGIIVEVTIKVYPLGQVLAGAIIYESSNLSAAIRHYNNGYHQLKQDYLPSS
LSLYQSVMNGPSGKALTVLFCWASSDMETGLLWLSKVQAFSPVAMCTVSPTTMAAFTLAT
ELLMPKSVHGTMLTANIHELTPEVVDVIGFHSSLQPNDSAIVFGIHELRVCTPVPSLDSV
IYTRSPHFVLEIGAIVETPHLLPDAIKWGQSFYNAVHKTDLANIMPSTYLPLTGPEKVDM
GAIYGPNLEVLRDIKQRYDPRDVFRHALVKV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	99	291	1.4e-47	0.43231441048034935

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.75e-24	100	281	31	224	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.01e-23	101	236	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.
178402	PLN02805	8.41e-07	100	265	133	309	D-lactate dehydrogenase [cytochrome]
183043	PRK11230	2.05e-05	99	266	54	233	glycolate oxidase subunit GlcD; Provisional
369658	BBE	3.04e-05	484	508	18	42	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI23960.1|AA7	5.11e-20	89	262	36	216
UPK90596.1|AA7	4.66e-18	101	262	20	188
UJO18775.1|AA7	1.61e-17	77	259	49	237
QRD93627.1|AA7	1.32e-16	101	506	48	466
UDD63515.1|AA7	1.32e-16	101	506	48	466

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	2.18e-25	101	276	39	219	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]
6FYD_A	6.52e-23	98	505	42	454	The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_B The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_C The crystal structure of EncM T139V mutant [Streptomyces maritimus],6FYD_D The crystal structure of EncM T139V mutant [Streptomyces maritimus]
6FYB_A	1.58e-22	98	505	42	454	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]
4XLO_A	2.12e-22	98	505	42	454	Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
6FYE_A	2.12e-22	98	505	42	454	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1RF55|AURO_GIBZE	1.49e-42	101	505	96	497	FAD-linked oxidoreductase aurO OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=aurO PE=1 SV=1
sp|P08159|HDNO_PAENI	1.11e-24	101	276	38	218	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|Q54H55|Y8969_DICDI	2.65e-19	95	506	42	443	FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
sp|M2T7Z1|TPCD_COCH5	1.18e-18	101	295	79	280	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A2V5HCN7|PYVE_ASPV1	2.03e-18	84	508	18	447	FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.999877	0.000144

TMHMM  Annotations     

There is no transmembrane helices in KAF7629516.1.