CAZyme Information: ASPCADRAFT_203113-t33_1-p1

Basic Information

• Species: Aspergillus carbonarius
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus carbonarius
• CAZyme ID: ASPCADRAFT_203113-t33_1-p1
• CAZy Family: GH15
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
568		61444.43	4.3982

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcarbonariusITEM5010	11735	602072	260	11475

• Gene Location: location=KV907494:94532-96238(-)

Full Sequence      

MTPSGYKASLAVLAAQILGVGAACGCECSLDSLNTTLQGRVQPLTPFSLPCFSNYNGQEV
TPNDAACANVQDNYTDPYLRTNSPNGYMNNQVEMCSSNPQDQCLLDSSDPTDPLAFVNQT
CRQGNMPSYYIEVTDDTDVREAMHFSNCSGTRLVIKNSGHDYLSRSSGKGTLALWTRKLQ
DLSYSSAFVPSGCQATYNAITAGAGVNFAEAYAFAHENNVTILGGYSPTVGLSGGWVMNG
GHSVLSPVYGLGVDRVVQYKIVTPDGQLRIANECQNQDLFWALRGGGGGTFGVVLESTHR
VEPTISFVAAIIKFTSNSTNVLPFMDIVVNNTLKWAQEGWGGHITGSTLVNVSPLLSVDE
AEESLAEVVAYAKAQGGSAVIEAFSSWYDFYEKYVTSTSVSVGVTHFAGSRLVPSSVFET
AEGRANLMDFFELILSNGQSPYIPVVGPVLYNYTEGSTSASPAWRQAIWELGSGSAWAWN
STLQTREQKIATLQNMTATLERITPGSGAYSNEANPFTEDWREAWWGDNYEKLLSIKEKY
DPTGLLSCWKCIGWEESQANSTCFAAFA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	127	309	6.6e-41	0.37554585152838427

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	9.33e-18	127	272	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	1.78e-13	200	546	97	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	5.69e-08	509	545	1	37	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	1.30e-05	113	275	8	158	UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].
273751	FAD_lactone_ox	1.46e-04	116	322	4	197	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	2.23e-42	33	546	518	1043
QKD57322.1|CBM91|GH43_11	2.23e-42	33	546	518	1043
UQC87672.1|AA7	4.43e-16	66	553	10	496
ADI58761.1|AA7|1.1.3.-	2.11e-13	138	542	48	460
AAS79317.1|AA7|1.1.3.-	4.05e-13	138	542	73	485

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	2.23e-68	33	562	46	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	1.75e-44	21	556	35	586	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	9.56e-16	127	545	45	452	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	2.25e-15	127	545	45	452	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	2.99e-15	127	545	45	452	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|A0A7L8UYL4|FFSJ_ASPFV	7.83e-170	31	562	27	596	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|G4MWA7|OXR2B_MAGO7	5.41e-143	31	567	30	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	2.91e-139	32	567	71	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	4.20e-124	31	452	26	422	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	1.15e-67	33	562	46	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 SP

Other	SP_Sec_SPI	CS Position
0.012002	0.987968	CS pos: 22-23. Pr: 0.9357

TMHMM  Annotations     

There is no transmembrane helices in ASPCADRAFT_203113-t33_1-p1.