CAZyme Information: ACLA_035090-t26_1-p1

Basic Information

• Species: Aspergillus clavatus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
• CAZyme ID: ACLA_035090-t26_1-p1
• CAZy Family: GH13
• CAZyme Description: FAD binding domain protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
645	DS027056|CGC3	68947.91	6.0407

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AclavatusNRRL1	9428	344612	287	9141

• Gene Location: location=DS027056:546585-548604(+)

Full Sequence      

MAPGRSVVLLATLALTTLCKADTTASRVAAEPVDAASTAADASLFPAETLQLTDSLLAHL
APVLANQSDLFAFGDTASSANLSVRGFNVCKTFPGDWFWPPPVVWSLVDRLLGGALIKTV
PLAAPCYSSWPEYNPTQCAAVTSNWTNSDMHAADPASVMWPLYEGRTCMPTSDPSGSCTV
GGYSSYAVNVSTVAQIQLAVNFARNMGLRLVVKNTGHDFSGKSTGAGALAIWTHHLKDLA
YLPNYQSARYTGPAVKMGAGVQAEQLYAMAQQLGFTAVGGEGKTVGVAGGYVLGGGHSPL
SSRYGLSADQVLALEVVLANGRFVTVTEETDPDLFWALRGGGGGTFGVVTSIISRVYPPV
GVTVSTFAFGTGPTVSADTFWAGVRAYFDRFAAHADAGTYAYFWVLPTGPRDFRFLMNPF
FAVNHTVAQCHALLQPWFDELDALAIPYTPNTTYYPTFHAAWQAGFPLESVALSTMMTGS
RLFPRANWEDPARLNQTFAALQATIRAGHPLLAFNLKAELAAGAAANAANPAFRSTLLHA
ITSTSWADAASPRDILQTMQTFATEVLDGWRQTCPDAGAYMSEATVLEPNFQQSFYGSHY
ARLYALKQRYDPFGLFYAPTAVGSEDWVVRSADGLPDQNGRLCRV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	188	618	4.6e-49	0.9497816593886463

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	2.70e-19	185	327	2	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	2.67e-11	182	333	30	176	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	1.94e-07	579	623	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.
273751	FAD_lactone_ox	4.97e-05	191	339	22	162	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
QKD57322.1|GH43_11	6.03e-68	90	644	500	1065
QKD57322.1|CBM91|GH43_11	6.03e-68	90	644	500	1065
AEO63154.1|AA7	7.29e-15	188	622	66	489
UJO23499.1|AA7	9.20e-14	195	380	74	254
UPK90596.1|AA7	2.40e-13	192	376	28	209

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	3.85e-104	90	645	28	574	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	1.46e-67	90	644	30	597	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	2.29e-21	191	412	52	262	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYF_A	4.09e-21	191	412	52	262	The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_B The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_C The crystal structure of EncM V135M mutant [Streptomyces maritimus],6FYF_D The crystal structure of EncM V135M mutant [Streptomyces maritimus]
6FYB_A	5.46e-21	191	412	52	262	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0E0RTV6|ZEB1_GIBZE	2.16e-118	90	644	27	562	FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2
sp|A1CFM2|PATO_ASPCL	4.99e-115	88	645	27	568	FAD-linked oxidoreductase patO OS=Aspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1 / QM 1276 / 107) OX=344612 GN=patO PE=1 SV=1
sp|A0A075TR33|PATO_PENEN	3.31e-108	90	645	28	567	FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1
sp|G0R6T3|SORD_HYPJQ	3.32e-105	72	645	20	573	FAD-linked oxidoreductase sor8 OS=Hypocrea jecorina (strain QM6a) OX=431241 GN=sor8 PE=3 SV=1
sp|G2QDQ9|VAO15_MYCTT	1.98e-103	90	645	28	574	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 SP

Other	SP_Sec_SPI	CS Position
0.000224	0.999752	CS pos: 21-22. Pr: 0.9743

TMHMM  Annotations     

There is no transmembrane helices in ACLA_035090-t26_1-p1.