CAZyme Information: P168DRAFT_332871-t37_1-p1

Basic Information

• Species: Aspergillus campestris
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
• CAZyme ID: P168DRAFT_332871-t37_1-p1
• CAZy Family: GT57
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
550	MSFM01000001|CGC26	60234.36	5.3037

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcampestrisIBT28561	9929	1392248	173	9756

• Gene Location: location=MSFM01000001:4549901-4551723(+)

Full Sequence      

MTDRLYGKTCNLPHFNATMQGRVQELKPFSLPCFSSYDGQSVGPNRAACAGIQQDYFNPW
ARTNSPNGYMNSQDEMCSSEPYNQCLLDDSNPANPTAYTNTTCRQGDLPSHYLEIQRVED
VIEAFKYAHCSGTKLSIKNSGHDYLGRSSGKDSLALWTRNLRSMSYSPDFVPSGCSAKYN
AITVGAGVNFDEVYAFADKHNVTLVGGYASTVGVSGGWVQNGGHSILSPVYGLGIDRVVD
YKIVTPDGQYRTANECQNPDLFWALRGGGGGTFGVVMESTHRVEPQIQLVAASIKFPKSP
TNVIPFLDIVVNHTLQWAAEGWGGHITGNTLVNVSPLLSVKEAKQSLAEAIAYAKSQGGT
AVVEEFPSWYPFYEKYVTSGSVGVGVTHFVGTRLVPKAVFQTAEGRKDLMDFFALLLDQG
QSPYIPVVGPVLFDYPEGSTSATPAWRSAVWELGVGASWAWNSTLQDRREKIATMKDTTA
FFARITPGSGAYANEASPFTEDWREAWWGDNYEELVSIKNKYDPFGLLSCWKCVGWTESQ
ADSSCFSAFV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	116	299	2.8e-43	0.3799126637554585

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	8.58e-20	109	254	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	4.63e-15	91	528	14	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	7.73e-09	109	308	15	201	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.
369658	BBE	1.67e-07	491	524	1	34	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.
223882	MurB	3.46e-07	101	257	13	158	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	7.72e-41	83	535	576	1050
QKD57322.1|CBM91|GH43_11	7.72e-41	83	535	576	1050
UPK90596.1|AA7	3.14e-13	109	529	20	436
AAS79317.1|AA7|1.1.3.-	1.12e-11	119	524	72	485
ADI58761.1|AA7|1.1.3.-	5.69e-11	119	524	47	460

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	1.64e-62	16	544	47	568	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6F74_A	1.79e-41	15	535	48	583	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	6.87e-18	120	528	56	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.63e-17	120	528	56	453	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]
2BVF_A	2.81e-17	120	524	50	444	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|A0A7L8UYL4|FFSJ_ASPFV	4.34e-167	16	535	30	587	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|G4MWA7|OXR2B_MAGO7	5.04e-150	19	549	36	580	FAD-linked oxidoreductase OXR2 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR2 PE=2 SV=1
sp|P0CU32|CHEF_CHAGB	3.18e-142	19	549	76	612	FAD-linked oxidoreductase cheF OS=Chaetomium globosum (strain ATCC 6205 / CBS 148.51 / DSM 1962 / NBRC 6347 / NRRL 1970) OX=306901 GN=cheF PE=2 SV=1
sp|Q0V6Q5|PHMC_PHANO	9.72e-112	16	433	29	421	FAD-linked oxidoreductase phmC OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=phmC PE=3 SV=2
sp|G2QDQ9|VAO15_MYCTT	8.45e-62	16	544	47	568	VAO-type flavoprotein oxidase VAO615 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=MYCTH_2305637 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P168DRAFT_332871-t37_1-p1.