CAZyme Information: P168DRAFT_313539-t37_1-p1

Basic Information

• Species: Aspergillus campestris
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus campestris
• CAZyme ID: P168DRAFT_313539-t37_1-p1
• CAZy Family: GT1
• CAZyme Description: FAD-binding domain-containing protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
520		56325.06	6.0635

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=MSFM01000015:529706-531398(-)

Full Sequence      

MKIPTILSFGALAAASSIDVCEKLHSHYPEYTVWDPLSPQGPESALNASMYRTARSEYWN
GVNARNRPACIFFPSNAEQVSDAVKHLNEYPNVEFALKSGGHNFNAGISSTAGGVLISFN
ENLSSATLSSDGKSFEVGPGARWGDVYEAGAKDNKIAVGGRLSNIGVGGFVLGGGLSYLS
AQYGLACDNVIDFEVVLGNGTVTHANSKTNPDLWWALKGGGNRFAIVTKFTLKAHPAGVD
GKVWGGIRFYSRNDRQAVFEAVSEFVRDYPDPKSAVIPTFDFGLPGAIVSNPALFFFYDG
PTPPAGAFGSLDKIKPLLNTTDTTTYPKLADQAGGGKIYGINAAARVNAFPNLDPKKTSE
LFEDHWKLYQDQIKNDSSRDIDIQIGTFTPQPVSVLIAKASQANGGNAMGLHPDHGDRIW
VENDLIWVNPVCNNACPTYLKNMGDGANAKFDEKFKGEKPTNYKSGDVEFISQNPLFMND
AADYQDVYSSYGEENKARLQKIAKAYDPKGFMKKQGGWDL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	58	514	1.2e-57	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.57e-21	59	512	23	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	7.96e-20	68	206	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.
215242	PLN02441	3.06e-07	33	237	33	241	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UJO16207.1|AA7	1.49e-20	68	230	128	289
UNI23960.1|AA7	2.25e-20	49	237	30	217
EGX49222.1|AA7|CBM1	2.15e-19	68	273	164	369
QMW30198.1|AA7	2.34e-19	47	237	28	217
QMW42271.1|AA7	2.34e-19	47	237	28	217

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO5_A	3.48e-21	37	265	18	242	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6EO4_A	3.48e-21	37	265	18	242	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
3W8W_A	1.87e-20	26	271	2	246	The crystal structure of EncM [Streptomyces maritimus],3W8W_B The crystal structure of EncM [Streptomyces maritimus],3W8X_A The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8X_B The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8Z_A The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus],3W8Z_B The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus]
6FYD_A	4.36e-20	59	271	37	242	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]
6FYG_A	7.81e-20	59	271	37	242	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|D4B1P2|A2372_ARTBC	1.89e-67	13	520	8	499	Uncharacterized FAD-linked oxidoreductase ARB_02372 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02372 PE=1 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	1.66e-53	51	520	65	513	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|M2T7Z1|TPCD_COCH5	5.22e-48	56	510	67	505	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	1.27e-46	48	520	25	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|G3Y424|YANF_ASPNA	1.03e-42	10	514	97	568	FAD-dependent monooxygenase yanF OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=yanF PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.006362	0.993589	CS pos: 15-16. Pr: 0.8624

TMHMM  Annotations     

There is no transmembrane helices in P168DRAFT_313539-t37_1-p1.