CAZyme Information: THC98252.1

Basic Information

• Species: Aspergillus tanneri
• Lineage: Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus tanneri
• CAZyme ID: THC98252.1
• CAZy Family: GT2
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:A0A4S3JRA7]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
570		64178.97	8.5970

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_AtanneriNIH1004	13590	N/A	33	13557

• Gene Location: location=SOSA01000049:45724-47436(-)

Full Sequence      

MSQTDFQPTGVTVYQPGHKEYELSVATSNLLYRFTRPPWVVKPKTTQEVEKIITEAQKNN
LSIAIKNGGHSGAGFSTTEQGVLVDLVNMNNVQLDMQSREPTATMGGGAKWGHAYRKLVN
GRHDGWVINGGRCPTVGVSGFVLGAGLCPFGRSIGMGCDRVTEITIVVPGKGAREAAKTL
TLKRGDTDANKRELFWALCGAGGGNFGIVTEVKMNVDNLGSLTVVAGRFIYQPRREDMAD
FMEMMNEFYTAKWSNEMTIDSSWLCDLNQTNSELAVRFIAYYKGNKGDFDREIDEKLVIG
ADVGKLLKRRSSEEKSTRFLHETLVSQWSEETIQSLPSSRTYSIYTSFVFSNDNKDQQIK
KITSIIRKEMKAFRTQFTGEQGLLQVTFLHSGGKAAEGPSTATAYPWRKGVYHTYITMQW
EDKWLKRDMQGFLAKFKKRLRPYSLCKEAVFINFADRELEADKYEAAYYGLHVARLKGIK
KYWDLTNFFKWQQGITLPEETSPDQTMARSLNEFARMEPKVKEEVLTQAEEDRQWDKVSL
PPASDFTGDIPLPWGVTIGSGIKSLHDLGF

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	36	495	1.2e-61	0.9694323144104804

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	6.66e-22	37	167	1	129	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	1.29e-17	36	230	31	217	FAD/FMN-containing dehydrogenase [Energy production and conversion].
369658	BBE	1.09e-07	450	495	1	44	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI23960.1|AA7	7.07e-20	37	495	48	469
QRC92907.1|AA7	1.43e-19	11	493	38	488
AEO63154.1|AA7	2.53e-19	11	495	37	489
QRW27390.1|AA7	1.42e-17	8	497	39	492
CCA69005.1|AA7	1.72e-17	9	502	31	491

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYE_A	6.62e-24	36	495	44	459	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.60e-23	36	495	44	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]
6FYG_A	2.88e-23	36	495	44	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]
6FYF_A	2.88e-23	36	495	44	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]
4XLO_A	5.17e-23	36	495	44	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	2.39e-22	1	495	1	442	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4
sp|Q0CF74|AZPB3_ASPTN	4.05e-22	10	489	38	474	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|Q9LPC3|BBE1_ARATH	7.65e-21	36	502	79	539	Berberine bridge enzyme-like 1 OS=Arabidopsis thaliana OX=3702 GN=SEC1A PE=2 SV=1
sp|Q33DQ2|CBCAS_CANSA	3.26e-20	18	495	56	537	Cannabichromenic acid synthase OS=Cannabis sativa OX=3483 GN=CBCAS PE=1 SV=1
sp|Q9FZC8|FOX5_ARATH	5.41e-20	40	495	80	522	Berberine bridge enzyme-like 7 OS=Arabidopsis thaliana OX=3702 GN=FOX5 PE=3 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000069	0.000000

TMHMM  Annotations     

There is no transmembrane helices in THC98252.1.