CAZyme Information: TRIREDRAFT_4114-t26_1-p1

Basic Information

• Species: Trichoderma reesei
• Lineage: Ascomycota; Sordariomycetes; ; Hypocreaceae; Trichoderma; Trichoderma reesei
• CAZyme ID: TRIREDRAFT_4114-t26_1-p1
• CAZy Family: GH16
• CAZyme Description: predicted protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
512		57444.31	6.7088

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TreeseiQM6a	9138	431241	7	9131

• Gene Location: location=GL985065:678350-679942(+)

Full Sequence      

MAPIPGVSGEQSEFGTASYEQWRQQYATSSHETDHDMHPGHIIRALNTKDIKAVIAYAKQ
NGKAIAIRSGGHQYSGASSTGQSNIQLDLRNTFKVPGEDLSLIHQGDETQVRTSVSWSLL
EINSFLGANHLFVPHGQCQSVCIGGHAQTGGYGQLGRSFGLMGDHIVKLEFIDHDGVERK
IAPASHPEEFFAWTGGSPGNLGVLTHITLKVYRDADYQGSRGLKGLHIYTPEALQKLLQV
LAEMNDDEEFPRNYDLCITVISEDYPLDGIFDLKRLTKQRTGLCRLDGASLLPLIVIYAQ
WVPFKSTDKPDETWFDKLKDGAVVNDDRVRPMSELTAEWIFRKDREYNLPYVKRTYATTA
TNLSKNGWVDWTAGRIDEVVKSTGNYIAAQIQPYGGKYARFRVNDDGRSAYSWRDSTMVL
GLDNFYVPGNGNKEDAEAWAAVNEHQGIGMNKYFSTQDRRVLWGSWGSYNLHSVWPCYYE
TEAKYKKLQRARKAADPYGVFTPNSFSVLRAD

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	35	213	1.8e-37	0.37117903930131

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.51e-17	25	217	15	209	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	2.33e-15	39	176	1	133	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	1.61e-04	98	213	196	306	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	0.002	50	211	26	178	sugar 1,4-lactone oxidases. This model represents a family of at least two different sugar 1,4 lactone oxidases, both involved in synthesizing ascorbic acid or a derivative. These include L-gulonolactone oxidase (EC 1.1.3.8) from rat and D-arabinono-1,4-lactone oxidase (EC 1.1.3.37) from Saccharomyces cerevisiae. Members are proposed to have the cofactor FAD covalently bound at a site specified by Prosite motif PS00862; OX2_COVAL_FAD; 1.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UKZ49297.1|GH31	2.14e-142	1	511	1	522
UKZ75824.1|GH31	4.86e-141	1	511	1	522
QYS96687.1|GH31	1.56e-139	1	511	1	522
UPK91582.1|GH31	3.31e-135	5	508	3	516
UPK90596.1|AA7	3.60e-13	39	212	20	187

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	2.34e-14	36	213	42	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]
6FYF_A	4.13e-14	36	213	42	210	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]
6FYE_A	4.13e-14	36	213	42	210	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	5.49e-14	36	213	42	210	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]
6FYG_A	5.49e-14	36	213	42	210	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|O64745|BBE16_ARATH	3.46e-13	39	213	83	253	Berberine bridge enzyme-like 16 OS=Arabidopsis thaliana OX=3702 GN=At2g34810 PE=2 SV=1
sp|Q9FZC8|FOX5_ARATH	1.05e-12	42	204	80	237	Berberine bridge enzyme-like 7 OS=Arabidopsis thaliana OX=3702 GN=FOX5 PE=3 SV=1
sp|Q9FZC5|FOX2_ARATH	4.29e-12	42	204	80	237	Berberine bridge enzyme-like 4 OS=Arabidopsis thaliana OX=3702 GN=FOX2 PE=2 SV=1
sp|Q9FZC6|FOX3_ARATH	7.49e-12	42	204	80	237	Berberine bridge enzyme-like 5 OS=Arabidopsis thaliana OX=3702 GN=FOX3 PE=3 SV=1
sp|Q9FZC7|FOX4_ARATH	1.38e-11	42	204	104	260	Berberine bridge enzyme-like 6 OS=Arabidopsis thaliana OX=3702 GN=FOX4 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000060	0.000000

TMHMM  Annotations     

There is no transmembrane helices in TRIREDRAFT_4114-t26_1-p1.