CAZyme Information: ASPBRDRAFT_117403-t33_1-p1

Basic Information

• Species: Aspergillus brasiliensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus brasiliensis
• CAZyme ID: ASPBRDRAFT_117403-t33_1-p1
• CAZy Family: AA16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
491		52733.30	4.1171

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AbrasiliensisCBS101740	13263	767769	274	12989

• Gene Location: location=KV878680:3569160-3570916(+)

Full Sequence      

MRIASLLPLTAAAAATATSAGCKALNKSLSSLVFAPSSTVYEYEAQNFWSNTELMSPGCV
FRPQSAEELSQGVKALVKANAQFAVRGGGHMGIRGSNNIDNGVLIVMSNLTTLELSDDRS
VVSVGPAYRWAAVYDYLETYDLAVAGGRLGPVGVPGLLLAGGINFFGNQVGFGCDTVINY
EVVLANGTIVEANATSHSDLFWALKGGSSNFGLVTRFDMETIESTQVWAGTYTVSAEYID
QFLEASATYAANISDPKTHIVPAVVPEGNTSVGSVILFYDSATESYPEIFKPFTDIPAVS
NTMGFKTLAEFAAETGAMVTPHINDIFVAGTIKATTYADLYRGISIINSTFAAQLPSLYA
QIPTANISIIELDWQPIGSSWLTASESRGGNALGLDKDQVYLCYAEVVEWIGSEYDEIVG
DWVVETTYKINNATLEAGLYDSFNYMGDAAWFQDIFDGYGAENLAKLQTIAKRYDPEGVF
QTLMPGGYKIF

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	46	481	2.4e-49	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.04e-20	57	193	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	1.58e-17	57	265	32	244	FAD/FMN-containing dehydrogenase [Energy production and conversion].
215242	PLN02441	1.51e-10	57	216	65	233	cytokinin dehydrogenase
178402	PLN02805	2.30e-04	57	215	134	298	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	0.006	43	203	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD93627.1|AA7	5.80e-21	30	487	21	474
UDD63515.1|AA7	5.80e-21	30	487	21	474
QMW46638.1|AA7	1.89e-20	30	487	21	474
QRC92907.1|AA7	4.99e-20	57	481	63	485
ADI58761.1|AA7|1.1.3.-	1.94e-19	57	480	37	464

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3HSU_A	1.87e-20	57	480	43	470	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	1.87e-20	57	480	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	2.04e-20	36	258	25	245	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	3.65e-20	36	258	25	245	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]
6FYG_A	3.65e-20	36	258	25	245	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|B6H064|PRX3_PENRW	1.49e-87	22	489	32	506	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	3.52e-85	22	490	32	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	3.52e-85	22	490	32	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|C8VPE5|SDCF_EMENI	3.09e-66	15	490	2	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	7.74e-66	45	490	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
0.735584	0.264435

TMHMM  Annotations     

There is no transmembrane helices in ASPBRDRAFT_117403-t33_1-p1.