CAZyme Information: ASPWEDRAFT_60249-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_60249-t33_1-p1
• CAZy Family: GT31
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
469	KV878212|CGC30	50332.86	8.7857

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AwentiiDTO134E9	12659	1073089	224	12435

• Gene Location: location=KV878212:4050100-4051738(+)

Full Sequence      

MIQYLLSAAPLLGLAAAANYSFPAVKNISQADIYQGNGPLPCEALIAAGLRDRVLLPADT
GYEPQVLSWWAWNSRQHPYCLVLPQNTQEVSLALTTLVHAGKGAGDWHIAVRSGGHSTIN
SNNIVNGVTIDLSHMNSSSYDESTNTARVQPGGRWQNVYADLQERNITVAGGRDGDVGVG
GFTLGGGNSFYSGRHSFACDTVNNFEVVLGNGTVVNANNKTNSDLYKALKGGTSNFGIVT
RFDFNAIPSLPLFHETRVMSANYTNIVLDAIVDYIRKLPAYVNKGGVDNMAAAAKASQFA
GESWNAGATVTFRNNPTILRYVNKLHDEYVKALQKSIGPDNFSTAIFLQPVPSYYAKISK
AHGGSMMPLEKLGGNAVMWTGGVAVKTTTGALAFAKAGMHQMAAKLTEFAKTVDGHVDMI
YLNYADATQDPLGSYGADRVEFMRKVAAKYDPAGVFQSRVPGGFKVNRV

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	68	252	2.3e-48	0.3930131004366812

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	7.20e-15	56	254	9	211	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	5.77e-14	78	218	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	2.46e-04	202	241	194	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRW22693.1|AA7	2.54e-16	51	251	34	231
AEO62186.1|AA7	8.24e-15	78	250	59	231
ANF89368.1|AA7	8.34e-15	78	267	61	250
AEO58513.1|AA7|1.1.3.-	8.34e-15	78	267	61	250
UJO23499.1|AA7	4.54e-14	57	249	42	231

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	5.83e-19	44	245	12	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]
6FYG_A	1.04e-18	44	245	12	207	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]
6FYF_A	1.04e-18	44	245	12	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]
4XLO_A	1.87e-18	44	245	12	207	Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
6FYE_A	1.87e-18	44	245	12	207	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0U5GQ05|DRTC_ASPCI	9.41e-72	42	469	45	516	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|C8VPE5|SDCF_EMENI	1.40e-64	42	468	8	478	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	9.24e-54	67	467	68	518	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|G3Y424|YANF_ASPNA	3.70e-49	62	457	138	567	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
sp|A0A2P1DP98|MACF_PENTR	3.73e-40	36	457	50	506	FAD-dependent monooxygenase macF OS=Penicillium terrestre OX=374132 GN=macF PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.457123	0.542869	CS pos: 17-18. Pr: 0.5078

TMHMM  Annotations     

There is no transmembrane helices in ASPWEDRAFT_60249-t33_1-p1.