CAZyme Information: ASPZODRAFT_151852-t33_1-p1

Basic Information

• Species: Penicilliopsis zonata
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Penicilliopsis; Penicilliopsis zonata
• CAZyme ID: ASPZODRAFT_151852-t33_1-p1
• CAZy Family: GH20
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
454		50762.20	5.5959

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PzonataCBS506.65	10027	1073090	158	9869

• Gene Location: location=KV878341:1429605-1431456(-)

Full Sequence      

MQIVRHSAPGYEEARIGRVFNARRPSRYPLAVVMARNTADVIEAVQLAIRSNCRVAIRSG
GHSWAAWSVRDNSVLIDLGEFKTLQVDPAALRARASPSITGKELNGRLVHEYGLMFPGGH
CPDVGLGGFLLQGGMGWNCRGWGWACERVEAVDVVTANGDLVHCNKDEHADLYWAARGAG
PGFPGVVVQFHLSLIKNPVFRSSGYLYPICEYRRAFDWILSLTPGYDADTEITVVAQYPE
GREELCLFILLVCMKPTAEEAEQALLPAQQSRPDGTVEEWFCKEDSLHAQYENQGKANPD
GHRYCADNAYLANETADVAAVLEEAFTTLPHRKAFALWYAMDPCSRRPLPDMALSLHSDH
YFALYTVWEDATDDERCTAWVQGVMQRVASHSVGAYLGDSDFQARQTQYWSEENTQRLTA
IRRKWDPEARICGYLGMEYVSSTRPWRDGVGSTL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	18	428	1.2e-74	0.9716157205240175

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	6.85e-24	29	165	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	1.50e-23	13	427	16	446	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHG26149.1|AA7	3.90e-23	29	198	42	213
UNI23960.1|AA7	4.56e-23	29	198	48	218
QUC19098.1|AA7	1.50e-22	29	198	48	218
BAI44126.1|AA7|CBM18	3.44e-22	16	198	263	444
QBZ61916.1|AA7|CBM18	3.44e-22	16	198	263	444

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	3.22e-35	2	427	21	449	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	8.37e-35	2	427	21	449	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	8.37e-35	2	427	21	449	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	1.15e-34	2	427	21	449	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
4XLO_A	1.15e-34	2	427	21	449	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0E3D8N6|PENO_PENCR	1.47e-102	8	431	16	437	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	1.47e-102	8	431	16	437	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	7.75e-99	11	433	22	442	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	2.48e-94	5	438	11	446	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A5ABH0|PYNB_ASPNC	9.88e-31	2	243	51	298	FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000034	0.000004

TMHMM  Annotations     

There is no transmembrane helices in ASPZODRAFT_151852-t33_1-p1.