CAZyme Information: P170DRAFT_448044-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_448044-t37_1-p1
• CAZy Family: GH5
• CAZyme Description: glycolate oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
600		66103.00	5.6150

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000005:2548255-2550279(-)

Full Sequence      

MSPSAFPVPKEPSELVPLLTESHHSGIPIRLASAAENAKSHYKSNSTVSGITPRDEDLPT
LPPGIERAQFNVAITDLESLVGSENVELNTQPLNDGWYMEHPNTHDAFHLLDPTNTVSSA
AVYPSSTEEVSAVVKWANHHEIPLWPISIGRNLGYGGAAPRVRGSVVVDLGRRMNEVLKI
DSVQLCCLVEPGVSYFKLYEEVQKSGYPLWIDTPDIGGGSVLGNAVDRGMGYTPMADHFA
NHCGLEVVLPNGNVLRTGMGALPGPNGQDNPTWQAFQYGYGPYIDGIFTQSNFGIVTKMG
MWLMPETDHLTFVVAFPEEEDLPEIIETVRQLMAKEIIQGSPQLRHVIQELTATGINRDE
LYPGDGQVPSDVIRLHASTLPCGDCSWVLYATLYGTPSQIQSDLTTAKSAFAQCPGSRVL
LPCDLPKSHYIHSCANVSSGVPEIRGLECLNWKHNGAHLFFSPICPPKGDDIRTIYGIVS
RIHRDHGLDIFPTFCVALREIHLIINIIYDRASLSEKQRAETVMTRMIDECAAAGYGDYR
THILFADQVAGAYSWNNHVLLKFHENMKDMLDEKGILAPGRNGIWPRKYREGLIANGFRS

Enzyme Prediction     

EC	1.1.3.38:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA4	60	591	9.4e-191	0.9865900383141762

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	5.66e-27	95	582	7	455	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	8.23e-27	119	258	2	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.
178402	PLN02805	2.91e-12	101	269	120	282	D-lactate dehydrogenase [cytochrome]
273750	pln_FAD_oxido	6.35e-04	118	209	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.
397178	FAD-oxidase_C	7.11e-04	491	580	140	246	FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKX53028.1|AA4	4.57e-308	9	590	3	585
BCS28313.1|AA4	9.65e-259	17	591	14	588
BCS25303.1|AA4	4.08e-233	13	591	2	578
AEO67281.1|AA4	3.82e-212	24	590	18	580
AEO65530.1|AA4	3.68e-211	149	590	1	442

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
1W1K_A	3.81e-152	60	589	11	553	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	1.52e-151	60	589	11	553	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	2.16e-151	60	589	11	553	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	2.16e-151	60	589	11	553	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]
1W1M_A	4.31e-151	60	589	11	553	STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant [Penicillium simplicissimum],1W1M_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Glu502Gly Mutant [Penicillium simplicissimum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|P56216|VAOX_PENSI	7.84e-151	60	589	11	553	Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
sp|P09788|DH4C_PSEPU	1.36e-110	55	584	3	515	4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
sp|P94535|GLCD_BACSU	1.28e-13	116	341	39	249	Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
sp|F1QXM5|LDHD_DANRE	2.08e-10	74	334	36	273	Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
sp|P9WIT1|Y2280_MYCTU	7.72e-10	121	334	43	240	Uncharacterized FAD-linked oxidoreductase Rv2280 OS=Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) OX=83332 GN=Rv2280 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000031	0.000000

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_448044-t37_1-p1.