CAZyme Information: AEO58370.1

Basic Information

• Species: Thermothelomyces thermophilus
• Lineage: Ascomycota; Sordariomycetes; ; Chaetomiaceae; Thermothelomyces; Thermothelomyces thermophilus
• CAZyme ID: AEO58370.1
• CAZy Family: GH18
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
574		61961.61	7.2073

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TthermophilusATCC42464	9292	573729	195	9097

• Gene Location: location=CP003004:4931334-4933233(-)

Full Sequence      

MPASLLRFLALAGTAVGLTTNHNHSPSCRVLPGDAAWPSSRDWAKLNKTLNGHLIATVPQ
ASVCHKSPFGQYDAQACEELKSSWDISTITHVNAPGDVLSQNFQNYSCVPFTDPSQPCQL
GNYPSYVVNVTGAADVQAALKFAQKHNVRIVIKNTGHDYLGKSTGKGALSLWMHNLKSTK
FIKNYKAPYYKGPAAKLGAGVEGFEAYAMANSTGHRIVGGTCPTVGIVGGYTQGGGHSIL
SSSYGVAADNVLEWEVVTADGRHLVATPTRNSDLYWALSGGGGGTFAVVLSMTARLHRDG
IVGGTLLGFNDSAVGNEVYWEAVAAFHALLPDFLDGGNSFTYSVGNNSLTAYGTMPGADR
DAVDRLLRPFLDDLASRGITPVVQPRVSTNYYDHFFTYLGPAPYGNAAYFPFTNSRIIPR
SLVTDPKSNAVVTDLFRNISQVPAFSPFYCDSFSVADKPHPANSLHPAWRTGMLLCAPAG
SWDWDASPEEMAARDRYAAETLQPMMDAATPGGSVYLNEANHLYANWKESFYGDNYARLL
RVKKKYDPDSVFYVKTGVGSEVWDVDATGRLCRA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	120	298	1e-46	0.37117903930131

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	2.91e-22	124	267	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.
223354	GlcD	1.96e-21	112	552	23	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	2.02e-11	515	559	1	45	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
239516	ADPRase_NUDT5	0.001	472	524	28	83	ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. Like other members of the Nudix hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue Nudix motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the Nudix motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer.
215242	PLN02441	0.005	218	283	171	226	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	3.75e-79	26	573	498	1065
QKD57322.1|CBM91|GH43_11	3.75e-79	26	573	498	1065
UQC87672.1|AA7	6.28e-19	124	560	70	497
BAI44126.1|AA7|CBM18	1.39e-16	124	553	275	711
RDX44700.1|AA7|1.1.3.-	1.53e-16	124	298	69	235

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	0.0	1	574	1	574	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]
6F74_A	3.16e-66	13	573	14	597	Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_B Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_C Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F74_D Crystal structure of VAO-type flavoprotein MtVAO713 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	1.78e-20	124	302	45	214	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYG_A	3.18e-20	124	302	45	214	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]
6FYD_A	4.25e-20	124	302	45	214	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|G2QDQ9|VAO15_MYCTT	0.0	1	574	1	574	VAO-type flavoprotein oxidase VAO615 OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=MYCTH_2305637 PE=1 SV=1
sp|A0A1V6PBT1|CALF_PENDC	2.76e-183	5	573	6	574	Bifunctional decalin synthase calF OS=Penicillium decumbens OX=69771 GN=calF PE=1 SV=1
sp|A0A0C6E5D0|BET5_NEOBT	1.10e-169	27	573	31	585	FAD-linked oxidoreductase orf1 OS=Neocamarosporium betae OX=1979465 GN=orf1 PE=3 SV=1
sp|A0A0E0RTV6|ZEB1_GIBZE	1.29e-143	23	574	22	563	FAD-linked oxidoreductase ZEB1 OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=ZEB1 PE=2 SV=2
sp|A0A075TR33|PATO_PENEN	2.84e-132	2	574	8	567	FAD-linked oxidoreductase patO OS=Penicillium expansum OX=27334 GN=patO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000344	0.999653	CS pos: 17-18. Pr: 0.9693

TMHMM  Annotations     

There is no transmembrane helices in AEO58370.1.