CAZyme Information: P168DRAFT_334825-t37_1-p1

Basic Information

• Species: Aspergillus campestris
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
• CAZyme ID: P168DRAFT_334825-t37_1-p1
• CAZy Family: GT62
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
503	MSFM01000011|CGC9	55257.97	5.7820

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AcampestrisIBT28561	9929	1392248	173	9756

• Gene Location: location=MSFM01000011:1500855-1502644(-)

Full Sequence      

MRLTSGVAAVLLGTLADYGQAKLSARSADPCCDALLLSKIGDRVVLPNVKSYKESVKSYW
AVNVQLEPNCIVQPVSTDEVSGAVQTLANSITGDSCKFAVRSGGHATWPGANNIEDGVTI
DLSNLNSTTYHKGAETAILHPGARWGDVYKALEPFGVTVPGGRTAPVGVGGFLLGGGNTF
HTARVGFATDNVENFEVVLASGRVVNANRQTNTDLYKALKGGTGNFGIVTKYDLKIIPHD
KLWGGLVGHENSTTPQLVDAFVNFVDHLHEDPYASYIGMWQYSTATKQNTVASALEYTKA
ETHPPAFHDFYHVKNVSDTMRLATMANLTAEIGQPDGYRDVFLTGTYENDAKILARAVKI
HDSKIDVLKSQAKSKDWTIYAMFQPWPKIFWEQSVKKGGNVLGLERNDKNLFQVLYDYSW
SDAADDELFRQTGIDALKELDEYAKSEGKYNEYVYLNYADRTQNPLRGYGPENLEYIKKV
AETYDPDGVFQTQVPGGFKITQE

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	58	492	1.1e-55	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.27e-23	64	490	28	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.28e-13	68	208	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.
178402	PLN02805	5.53e-08	61	238	130	308	D-lactate dehydrogenase [cytochrome]
215242	PLN02441	1.61e-06	64	231	61	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW22693.1|AA7	9.65e-19	10	491	7	477
CDR44461.1|AA7	1.12e-17	2	264	3	261
CCA70426.1|AA7	1.47e-15	31	232	57	255
QRD93627.1|AA7	2.24e-15	36	238	13	215
UDD63515.1|AA7	2.24e-15	36	238	13	215

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO5_A	2.10e-23	22	240	8	217	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	2.10e-23	22	240	8	217	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6FYD_A	2.20e-20	29	236	7	208	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	3.95e-20	29	236	7	208	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	3.95e-20	29	236	7	208	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|C8VPE5|SDCF_EMENI	4.24e-163	31	500	8	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|A0A0U5GQ05|DRTC_ASPCI	3.46e-133	15	502	30	515	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	4.94e-87	11	500	3	517	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0A023I4D6|PRX3_PENRO	3.67e-64	21	500	22	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	3.67e-64	21	500	22	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000440	0.999533	CS pos: 21-22. Pr: 0.9677

TMHMM  Annotations     

There is no transmembrane helices in P168DRAFT_334825-t37_1-p1.