CAZyme Information: ASPTUDRAFT_175347-t33_1-p1

Basic Information

• Species: Aspergillus tubingensis
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tubingensis
• CAZyme ID: ASPTUDRAFT_175347-t33_1-p1
• CAZy Family: GH13
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
575		65032.57	7.0367

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtubingensisCBS134.48	12592	767770	274	12318

• Gene Location: location=KV878205:911729-913513(+)

Full Sequence      

MGDIGTHPRWKDPEIQHQVDLALLEDEASQREADEARRKVVPLLSRLHRGSVLFPRSQGY
RYSVSVRNLRYRLKRPAAVVHAVTAWDVVATVRFCVQEGLKLTIRSGGHSNAAHCLNDNG
IVLDMRMLNKVVIQPNHDIIYVSGGALWRDVYKELHDRDPRLVVVGGQCPTVGVSGFLLG
GGISPFSRSYGLGIDNIEAIEIVKANGELCIVSADNHPDLFWALRGGGGGNFGVATGFFL
KVHTLNHPEGMVTCGTLGWSVEDTKSRKKFIDTMKNWDQTPLPPALCGDALWRYRRDRET
KEKRLWAEITIMYNGGKNDCDSELAKILRGKPDVNTLKEMKFYDWEVGGEAFSNHSQVHQ
HHSSVIIEKGHVLESENGRCHVLWDHIGEQTSQKKPDETAFPWRTGEYALSMKASWDNED
KEKEMIREVQRLRDELTKYAIGGKAAYVNFIDNTLSGWWDAYYDTNYERLRQVKEIYDPE
EFFEFQQSIRKPQSDYPQITAVPSRTAAVHLPELDEKKDFLEDIEKGTTRTEKPFPQDAP
AQSVSDLGYGGLHSGRCPAVSLKRYILGLVSRLKS

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	67	489	7.3e-74	0.9868995633187773

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	4.67e-33	43	479	2	446	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	4.80e-29	76	213	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	1.65e-14	76	223	65	220	cytokinin dehydrogenase
369658	BBE	1.65e-14	446	490	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.
273751	FAD_lactone_ox	3.92e-04	87	225	26	162	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
QRW00715.1|AA7	3.16e-30	50	489	40	489
QRW15212.1|AA7	3.16e-30	50	489	40	489
QRV86657.1|AA7	3.16e-30	50	489	40	489
QRD00400.1|AA7	8.01e-29	76	490	46	473
QRW22693.1|AA7	3.74e-28	51	489	36	482

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYE_A	6.07e-37	49	489	19	459	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.55e-36	49	489	19	459	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	2.89e-36	49	489	19	459	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]
6FYG_A	3.95e-36	49	489	19	459	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]
4XLO_A	5.40e-36	49	489	19	459	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|Q796Y5|YGAK_BACSU	2.75e-47	62	489	18	442	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
sp|O06997|YVDP_BACSU	1.92e-37	50	489	8	443	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1
sp|F4HV09|BBE14_ARATH	1.80e-31	66	489	65	521	Berberine bridge enzyme-like 14 OS=Arabidopsis thaliana OX=3702 GN=At1g34575 PE=3 SV=1
sp|P08159|HDNO_PAENI	6.81e-31	50	260	13	216	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2
sp|Q9SA86|BBE9_ARATH	1.14e-30	66	489	68	525	Berberine bridge enzyme-like 9 OS=Arabidopsis thaliana OX=3702 GN=At1g30710 PE=2 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000050	0.000001

TMHMM  Annotations     

There is no transmembrane helices in ASPTUDRAFT_175347-t33_1-p1.