CAZyme Information: PV06_06581-t43_1-p1

Basic Information

• Species: Exophiala oligosperma
• Lineage: Ascomycota; Eurotiomycetes; ; Herpotrichiellaceae; Exophiala; Exophiala oligosperma
• CAZyme ID: PV06_06581-t43_1-p1
• CAZy Family: GH32
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
603		66721.92	7.5156

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_EoligospermaCBS72588	11938	N/A	45	11893

• Gene Location: location=KN847337.1:290283-292150(-)

Full Sequence      

MSSRSLPVTPTLEEKHSGIPTRLVEQAKRAKELLFSRRTKTENTSSSRRRVQLPPYTTQA
KFDNAITALKAAVGAQYVCVNDGALVDGWYMEHPNTHDSNHVANQDALVASAVVYPSTTE
EVQAIVKWANEFLIPIHPISMGRNLGYGGAAPRVSGSVVVDLGKRMNKILKIDGQNYSCL
LEPGVSYFALYEAVKKSGHSLWIDCPDLGGGSVMGNALDRGVGYTPYGDHFGMHCGMEVV
LPDGTLLRTGMGALPGEDDTDNLTWQSFQNAYGPAIDGMFSQSNYGIVTKMGFWLMPATG
SQSYLVTFPREDDFEQLVDLIGPLAASRVFGNVPQIRHVVQELAVTGKPRSHFWPEGNDK
GGRMPRSVISREAAKLPCGDVSWIFYGCQYGDPATIQSQLDLIKTTFAKVKGSKFYLPSD
LPDDHYIHERAKVNMGEPVLKELDWLNWLPNGGHIACSPILPTTGKHARTMMTIAERLYA
KWGFDSFSTLCVAGREMHFISEIVFDREDADSKRRAACLMRELIDEGAQKGYGEYRTHLL
YMDQVAGTYKWGNGALGRFNETIKDALDPNGIISPGRNGIWGKRWREKGWKSGQVGMPRE
VKL

Enzyme Prediction     

EC	1.1.3.38:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	52	590	4.7e-199	0.9923371647509579

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	6.27e-31	110	250	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	4.33e-26	87	578	9	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402	PLN02805	7.49e-08	93	253	120	274	D-lactate dehydrogenase [cytochrome]
183043	PRK11230	1.61e-05	113	258	59	205	glycolate oxidase subunit GlcD; Provisional
273750	pln_FAD_oxido	0.001	110	201	32	123	plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BCS28313.1|AA4	2.59e-288	5	591	9	592
QKX53028.1|AA4	2.29e-244	5	591	6	590
AEO65530.1|AA4	1.45e-228	141	591	1	447
QGA17285.1|AA4	6.51e-222	1	591	1	582
AEO67281.1|AA4	6.98e-221	10	591	12	585

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W1K_A	2.06e-166	49	591	8	559	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum],1W1K_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Ile238Thr Mutant [Penicillium simplicissimum]
1AHU_A	1.65e-165	49	591	8	559	Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHU_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With P-Cresol [Penicillium simplicissimum],1AHV_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHV_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 2-Nitro-P-Cresol [Penicillium simplicissimum],1AHZ_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1AHZ_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With 4-(1-Heptenyl)phenol [Penicillium simplicissimum],1VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],1VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-alcohol Oxidase [Penicillium simplicissimum],2VAO_A Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum],2VAO_B Structure Of The Octameric Flavoenzyme Vanillyl-Alcohol Oxidase In Complex With Isoeugenol [Penicillium simplicissimum]
1W1L_A	1.65e-165	49	591	8	559	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum]
1E8F_A	1.65e-165	49	591	8	559	Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8F_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form [Penicillium simplicissimum],1E8G_A STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8G_B STRUCTURE OF THE H61T DOUBLE MUTANT OF VANILLYL-ALCOHOL OXIDASE IN COMPLEX WITH FLUORO-CRESOL [Penicillium simplicissimum],1E8H_A Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum],1E8H_B Structure Of The H61t Mutant Of The Flavoenzyme Vanillyl- Alcohol Oxidase In The Apo Form Complexed By Adp [Penicillium simplicissimum]
5MXU_A	6.62e-165	49	591	8	559	Structure of the Y503F mutant of vanillyl alcohol oxidase [Penicillium simplicissimum],5MXU_B Structure of the Y503F mutant of vanillyl alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P56216|VAOX_PENSI	8.50e-165	49	591	8	559	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
sp|P09788|DH4C_PSEPU	5.81e-103	53	580	9	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|P94535|GLCD_BACSU	8.92e-12	112	398	43	309	Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
sp|D4MUV9|DLD_ANAHA	8.59e-11	113	577	51	470	D-lactate dehydrogenase OS=Anaerostipes hadrus OX=649756 GN=CL2_23160 PE=1 SV=1
sp|Q86WU2|LDHD_HUMAN	2.84e-10	66	298	32	265	Probable D-lactate dehydrogenase, mitochondrial OS=Homo sapiens OX=9606 GN=LDHD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000047	0.000000

TMHMM  Annotations     

There is no transmembrane helices in PV06_06581-t43_1-p1.