CAZyme Information: P170DRAFT_490652-t37_1-p1

Basic Information

• Species: Aspergillus steynii
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus steynii
• CAZyme ID: P170DRAFT_490652-t37_1-p1
• CAZy Family: GT32
• CAZyme Description: FAD dependent oxidoreductase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
494	MSFO01000002|CGC6	54493.19	4.7544

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AsteyniiIBT23096	13430	1392250	235	13195

• Gene Location: location=MSFO01000002:6028226-6030007(+)

Full Sequence      

MTRTSVWRTAIAACLAAFATADVCSKLEAEGIPIDKRLTIDYHQDLKDYWSTACGDLRPT
CIAAPSSAFEMSQIVKELHNFNTSFAVKSGGHMPNNGFASIQDGLLVSTKNLNDVVYNPD
DRTAIIGPGLSWEEAQKGLDDVDAGRALVGGRLGGVGVGGYMLGGGLSFLSSQYGWAANN
VVNFEVVLANGTIVNANKDENEDLFGVLKGGGSNFGIVTAYTLETHPIGKVWGGNYIFKA
SQTAEVLEAVRDFTDNYPDDKAAVIVTAEHAALLNTWIMFLFYDGPEPPNGVFDKFKALK
PTDTTKTWDSYYDLLKNNDFFILKGQRYTIATETTPVPDKSAGKEVMQTYYDHWFNVTKS
VIDVPGVIGSLAFQPMPGAITKKAKAKGGDLYNFPTDTNYIVLELDFSYLFPASDKRIDE
ANRRLFNGFDEHISEFVDQGVLPDVRRPIFLNDANYAQDYWGRSESTQHAREVREIYDPD
MFFQKRTSGGFRLG

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	55	272	1.1e-53	0.47161572052401746

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	7.37e-16	58	289	31	281	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.01e-12	59	197	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	7.33e-04	59	228	134	307	D-lactate dehydrogenase [cytochrome]
215242	PLN02441	0.001	179	219	192	232	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CAI94231.1|AA7|1.1.3.-	1.87e-23	27	253	29	258
UJO18775.1|AA7	1.97e-21	59	244	73	263
UNI23960.1|AA7	3.53e-19	59	227	48	216
UPK90596.1|AA7	4.05e-19	59	227	20	188
UJO23499.1|AA7	6.90e-19	59	227	63	230

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3RJ8_A	5.22e-25	27	363	7	350	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]
6FYD_A	2.92e-18	56	260	42	243	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	5.21e-18	56	260	42	243	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	5.21e-18	56	260	42	243	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]
6FYB_A	9.29e-18	56	260	42	243	The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|D4B1P2|A2372_ARTBC	2.20e-150	23	494	28	500	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|A0A023I4D6|PRX3_PENRO	1.47e-50	42	493	51	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti OX=5082 GN=prx3 PE=3 SV=1
sp|W6Q5R7|PRX3_PENRF	1.47e-50	42	493	51	507	FAD-dependent monooxygenase prx3 OS=Penicillium roqueforti (strain FM164) OX=1365484 GN=prx3 PE=3 SV=1
sp|A0A0U5GQ05|DRTC_ASPCI	2.44e-48	19	493	40	513	FAD-dependent monooxygenase drtC OS=Aspergillus calidoustus OX=454130 GN=drtC PE=1 SV=1
sp|B6H064|PRX3_PENRW	2.78e-48	42	493	51	507	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

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000255	0.999716	CS pos: 21-22. Pr: 0.9668

TMHMM  Annotations     

There is no transmembrane helices in P170DRAFT_490652-t37_1-p1.