CAZyme Information: ATCC64974_56210-t41_1-p1

Basic Information

• Species: Aspergillus niger
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus niger
• CAZyme ID: ATCC64974_56210-t41_1-p1
• CAZy Family: GH3
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
509	OGUI01000007.1|CGC27	55182.12	5.0745

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=OGUI01000007.1:4257632-4259344(+)

Full Sequence      

MKFLLLLASLAFSALGSSLVGSGQRGINTTSTTTISTVDLETGAKCACTKLAGLYSNLVL
YPESANYTSQATSYWDIRADLDPACIFLPTSAEQVADAVGLFATCGTQFAVRGGGHMNYP
GSNNINGGVLLAFDNMKQYRVNNETIEVTPGMTWYDVYSALDPYGRAAIGGRLKTIGVPG
LTLIGGVSYFINKYGFAMDNVVNYDIVLGNGTQVAANATSNPDLFWALKGGANNFGIVTK
FTLKTYSMPHISTTIQEFNETAVHDFIKASCDWVVADGDSSIAAGSVLTITYNATTGSVS
PLLLGVQEGISNPPSKFANFTAIPGVYKVNNVTTSKQWAANLDSPKQMFRVTFGHHSMYP
DSDVLYSMYQTWKAAVNQIADVQGLYPTFVINISPSSAVRVGNTNGIGNVWGLAEEPTIW
WQLSTGWDNAEDDLRVEAWVRQLVEHLHGINKSNGLARDFIYMGDGGDWQDPFAGFPGEN
VQRMREIRERYDPLGTFTRLNWGGFKLGN

Enzyme Prediction     

No EC number prediction in ATCC64974_56210-t41_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	71	498	5.3e-57	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	5.07e-24	83	497	32	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.39e-21	83	214	1	136	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	1.56e-08	83	240	65	233	cytokinin dehydrogenase
178402	PLN02805	7.08e-08	83	287	134	341	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	2.29e-06	83	254	15	187	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD93627.1|AA7	1.47e-25	56	256	21	222
UDD63515.1|AA7	1.47e-25	56	256	21	222
QMW46638.1|AA7	4.89e-25	56	256	21	222
ADI58761.1|AA7|1.1.3.-	5.26e-24	63	273	18	233
AAS79317.1|AA7|1.1.3.-	1.56e-23	63	273	43	258

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HSU_A	5.54e-25	63	273	24	239	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	5.54e-25	63	273	24	239	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]
6FYE_A	1.09e-23	59	501	22	456	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	2.64e-23	59	501	22	456	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]
6FYF_A	4.78e-23	59	501	22	456	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	3.26e-75	47	509	31	509	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|A0A023I4D6|PRX3_PENRO	3.48e-74	47	509	31	509	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	3.48e-74	47	509	31	509	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A2G5ICA0|CTB5_CERBT	1.95e-55	20	507	23	524	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|M2T7Z1|TPCD_COCH5	1.18e-54	47	507	33	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 SP

Other	SP_Sec_SPI	CS Position
0.000247	0.999727	CS pos: 16-17. Pr: 0.9738

TMHMM  Annotations     

There is no transmembrane helices in ATCC64974_56210-t41_1-p1.