CAZyme Information: ASPWEDRAFT_29799-t33_1-p1

Basic Information

• Species: Aspergillus wentii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus wentii
• CAZyme ID: ASPWEDRAFT_29799-t33_1-p1
• CAZy Family: GH3
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
493		53198.56	4.5882

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=KV878214:132540-134108(-)

Full Sequence      

MSFVRLALVASIFSSWVTLGLASDTTNPCDELSNSLPGKVVLPGNPQYQSDVSSYFFLNQ
RIDPFCIVVPTSAEDVSLSVKILTKHPSTPFAIRGGGHSPNRGASNAENGVTIDFQSMKE
VANYGPITSVGPGAAWSDVYSVLDPKGLTVVGGRVAGVGVGGLTTGGGISAFSPELGFAC
DNVANMQVVLANGEIVNANATSNADLFIALKGGQNNFGIVTRFDLKTHQRDEYWGGSINY
PQEAEAAQLAAFTEFKDPANFDQYAEIEQSFLYIGQEKAFYSSNNMYYTKPVVNATGLKY
FTDVQPQVSSTMRIANTSSFAEELASVQPQNQFHSAEWATTTFAISPTILGKVHGLWNAS
AVELTPVTNLTSVLTFQSVPAPQPSSPNSLGIDPKSSPEKNLVLALVNQYWSLESDSDKA
NGVTEELMSNIDDLLRQEGLYVDYKYLNYAGPFQDPLGSYGDESLERMKKVSTKYDPTGV
FQKQVKGGFKLFK

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	63	257	7.9e-52	0.4279475982532751

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.11e-17	61	481	29	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.96e-17	64	199	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	9.45e-14	1	222	5	233	cytokinin dehydrogenase
178402	PLN02805	2.84e-07	64	233	134	310	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD93627.1|AA7	2.27e-22	40	228	24	214
UDD63515.1|AA7	2.27e-22	40	228	24	214
QMW46638.1|AA7	7.44e-22	40	228	24	214
UNI23960.1|AA7	4.27e-21	34	298	18	285
RDX44700.1|AA7|1.1.3.-	9.89e-20	2	480	7	503

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6EO4_A	7.35e-19	39	228	24	216	Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens],6EO4_B Physcomitrella patens BBE-like 1 wild-type [Physcomitrium patens]
6EO5_A	7.35e-19	39	228	24	216	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]
6F72_A	5.63e-18	14	481	82	552	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYD_A	1.23e-17	33	229	15	210	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]
3RJ8_A	1.29e-17	42	246	16	226	Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|C8VPE5|SDCF_EMENI	1.13e-72	29	491	9	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	2.04e-69	29	493	45	515	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|A0A2G5ICA0|CTB5_CERBT	2.24e-69	14	491	33	524	FAD-dependent monooxygenase CTB5 OS=Cercospora beticola OX=122368 GN=CTB5 PE=3 SV=1
sp|M2T7Z1|TPCD_COCH5	7.37e-68	50	491	63	517	FAD-dependent monooxygenase tpcD OS=Cochliobolus heterostrophus (strain C5 / ATCC 48332 / race O) OX=701091 GN=tpcD PE=1 SV=1
sp|A0ST43|CTB5_CERNC	7.69e-66	52	491	1	456	FAD-dependent monooxygenase CTB5 OS=Cercospora nicotianae OX=29003 GN=CTB5 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.001345	0.998624	CS pos: 22-23. Pr: 0.9718

TMHMM  Annotations     

There is no transmembrane helices in ASPWEDRAFT_29799-t33_1-p1.