CAZyme Information: P175DRAFT_0492612-t39_1-p1

Basic Information

• Species: Aspergillus ochraceoroseus
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus ochraceoroseus
• CAZyme ID: P175DRAFT_0492612-t39_1-p1
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
440		49461.25	5.1898

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AochraceoroseusIBT24754	9070	1392256	153	8917

• Gene Location: location=MSFN02000003:2122339-2123763(-)

Full Sequence      

MDIVWREKNDPAIYEAARTKRLFNAQVPDRYPLAIAFVESDIHIVDAVRLAIDQKCQISV
RAGGHSFPAWSVCENAILVDLGNFSEIVMDDETGVVGVTPATTSRKLNEFLSVKGRIASV
GHCPDVGLGGFLLAGGLGWNSRNWGWACEQIVAVDVVTPGGELLRADREKNTELFWAVRG
GGPAFPGIITRFYLQTRPAPRRILSSVYVYPVTHCGEAFSWILDIGSELRGNIEISAVAT
YVPEQETPCLIIKMMAFGDEEESVKQLQRAENSYPPGSLSHSFCQETTLQNEFDNMEIAF
PSNHRYCVDNAFLRNDIDVAALLQTAFTTLPSKKSMVLWNFMMPRSQRELLDMALSIQSN
HYCAVYAIWEDESEDGYCRSWVQTIMRGLETHSIGSYVGEYDFQARACNVWGAEQYERLK
HIKQKWDPHNRMCPCPGLRL

Enzyme Prediction     

No EC number prediction in P175DRAFT_0492612-t39_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	19	432	1.5e-73	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.79e-22	16	434	16	452	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	3.22e-17	32	167	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.
215242	PLN02441	8.26e-06	150	202	190	244	cytokinin dehydrogenase
273751	FAD_lactone_ox	1.65e-04	44	199	27	181	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
CBX96933.1|AA7|CBM18	1.52e-29	23	210	205	393
QRD00400.1|AA7	2.81e-26	8	213	25	228
CAK49173.1|AA7	3.48e-26	32	224	47	241
UDD61931.1|AA7	3.52e-26	32	224	48	242
CAE7194773.1|AA7|CBM18	3.72e-26	2	210	109	315

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	7.70e-33	2	430	21	451	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]
6FYG_A	1.99e-32	2	430	21	451	The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_B The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_C The crystal structure of EncM V135T mutant [Streptomyces maritimus],6FYG_D The crystal structure of EncM V135T mutant [Streptomyces maritimus]
6FYF_A	1.99e-32	2	430	21	451	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]
6FYE_A	2.72e-32	2	430	21	451	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	2.72e-32	2	430	21	451	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|A0A0E3D8N6|PENO_PENCR	2.60e-105	4	432	12	437	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	2.33e-103	2	432	8	437	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	2.78e-101	1	432	9	440	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	2.86e-98	1	432	6	439	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|I1SB12|MNCO_MICNN	3.94e-25	11	431	39	484	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000076	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P175DRAFT_0492612-t39_1-p1.