CAZyme Information: ATCC64974_59580-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ATCC64974_59580-t41_1-p1
• CAZy Family: GH31
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
494	OGUI01000008.1|CGC8	53080.57	4.0592

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AnigerN402ATCC64974	11187	N/A	0	11187

• Gene Location: location=OGUI01000008.1:227081-228836(-)

Full Sequence      

MRIASLLPLTAAATTVAAKATSAGCKALNKSLSSAVFAPSSTVYQYEAQNFWSNTEIMSP
GCVFRPQSAEELSQGVKALVDAEAQFAVRGGGHMGIRGSNNIDNGVLIVMSNLTTLELSD
DQSVVSVGPAYRWAAVYEYLENYNLAVAGGRLGPVGVPGLLLAGGINFYGNQVGFGCDTV
INYEVVLANGTIIEANATSHSDLFWALKGGSSNFGLVTRFDMETIESTQVWAGTYTVAAE
YIDQFLEASATYAANISDPKTHIVPAVVPEGNTSVGSVILFYDSATESYPEIFKPFTDIP
AESNTLGFKTLAEFAAETGAMVTPHINDIFVAGTIKATTYADLYRGISIINSTFAAQLPS
LYAQIPTANISIIELDWQPIGASWLEASESRGGNALGLDKDQVYLCYAEVVEWIGSEYDE
IVGEWVVETTYKINNATLEAGLYDSFNYMGDAAWFQDIFDGYGEENLAKLQTIAKKYDPN
GVWQGLMPGGYKIF

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	48	483	5.1e-49	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	7.65e-20	60	196	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	6.87e-18	60	268	32	244	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	1.99e-09	60	219	65	233	cytokinin dehydrogenase
273751	FAD_lactone_ox	1.36e-04	46	206	2	160	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.
178402	PLN02805	1.79e-04	60	218	134	298	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD93627.1|AA7	4.42e-21	33	490	21	474
UDD63515.1|AA7	4.42e-21	33	490	21	474
ADI58761.1|AA7|1.1.3.-	7.82e-21	60	483	37	464
QMW46638.1|AA7	1.44e-20	33	490	21	474
AAS79317.1|AA7|1.1.3.-	2.19e-20	60	483	62	489

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HSU_A	7.73e-22	60	483	43	470	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	7.73e-22	60	483	43	470	The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
6FYD_A	5.13e-19	39	223	25	207	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]
5K8E_A	8.00e-19	6	224	3	227	Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]
6FYF_A	9.17e-19	39	223	25	207	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6H064|PRX3_PENRW	2.51e-86	25	493	32	507	FAD-dependent monooxygenase prx3 OS=Penicillium rubens (strain ATCC 28089 / DSM 1075 / NRRL 1951 / Wisconsin 54-1255) OX=500485 GN=prx3 PE=2 SV=1
sp|W6Q5R7|PRX3_PENRF	2.12e-84	25	493	32	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A023I4D6|PRX3_PENRO	2.12e-84	25	493	32	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|C8VPE5|SDCF_EMENI	5.84e-68	25	493	9	476	FAD-dependent monooxygenase sdcF OS=Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) OX=227321 GN=sdcF PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	9.15e-64	48	493	66	517	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.692464	0.307533

TMHMM  Annotations     

There is no transmembrane helices in ATCC64974_59580-t41_1-p1.