CAZyme Information: ASPWEDRAFT_40673-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_40673-t33_1-p1
• CAZy Family: GH5
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
459	KV878212|CGC4	52385.12	6.5512

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AwentiiDTO134E9	12659	1073089	224	12435

• Gene Location: location=KV878212:2163275-2164782(+)

Full Sequence      

MQIIWRNSTDKPTYEEARIGRVFNHRRPPRYPIAIAKPTTEEDIIAAVKLAAAHKCRVAV
RSGGHSWAAWSVRDHSILIDLGGYKHLEVDAENRVARASPSLTGREINGVLTGEYGMMFP
GGHCPDVGLGGFLLQGGMGWNCRNWGWACERVEAVDVVTAAGELLHCNAQQNRDLYWAAR
GAGPGFPGIVTKFHLQLIPYPQRGFRSSGYIYPIRQYKEAFNWILSITPTFDQDTEIAAV
AHYAPDNSEEMYFFILFVVMKDDPHEAENALRPAQQTRPPGCITEWFCQEDSLENQYVNQ
GKANPEMHRYCAENAYIQNEANVPDVLEEAFTTLPHQKAFALWYPMNPCSRRKLPDMALS
MQSDHYFALYTVWEDEKDDVRCQTWVRETMKKVERHSVGSYLGDADFQVRKSRYWADDNA
RRLMAIRRKWDPEGRICGYLTLGDDSGTRGLDNAHEWKL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	21	434	7.5e-79	0.9737991266375546

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	2.42e-26	16	435	16	449	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.31e-22	32	168	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	6.80e-04	156	203	198	244	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAI44126.1|AA7|CBM18	3.29e-25	19	196	263	439
QBZ61916.1|AA7|CBM18	3.29e-25	19	196	263	439
RDX44700.1|AA7|1.1.3.-	5.07e-25	32	193	69	229
ATZ50592.1|AA7	5.54e-25	32	201	70	240
QRW06655.1|AA7	8.79e-25	8	201	47	238

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.85e-35	2	432	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	4.81e-35	2	432	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	4.81e-35	2	432	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]
6FYB_A	6.61e-35	2	432	21	449	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]
6FYE_A	6.61e-35	2	432	21	449	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0E3D8N6|PENO_PENCR	1.22e-105	4	436	12	437	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	3.44e-105	4	436	12	437	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	9.40e-105	1	438	6	441	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	2.04e-100	1	438	9	442	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A5ABH0|PYNB_ASPNC	5.71e-29	13	237	59	282	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
1.000062	0.000000

TMHMM  Annotations     

There is no transmembrane helices in ASPWEDRAFT_40673-t33_1-p1.