CAZyme Information: TSTA_061230-t26_1-p1

Basic Information

• Species: Talaromyces stipitatus
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces stipitatus
• CAZyme ID: TSTA_061230-t26_1-p1
• CAZy Family: GH28
• CAZyme Description: FAD binding oxidoreductase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
462		52074.10	6.4386

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TstipitatusATCC10500	12629	441959	146	12483

• Gene Location: location=EQ962652:431832-433425(-)

Full Sequence      

MSNMYLLAYSRRSTKPDQPLSIIWRGQVNESVYEEARVKRIFNCQRPTRYPQAIIFAKTE
SDIINAVNLAIDQKYSISIRAGGHSWPVWSLRDDTILMDLGCLSDISLDEETGVVRVSPS
TTGKELSDYLHAKGRTFPVGHCPDVGLGGYLLCGGMGWNSNNWGWACEYVVAVDVVTSTG
EIVHADVEQNNDLFWATRGSGPGFPGIVTRFHLQSRLLPKIMKSSLYIYTMKHYQPVFDW
ALKIPSGIDEGLEIAVIGSYPPEFNEPCITVALLALGDSDESVIKVLRRADESHPDGAVT
RSFCGNTSFNEQFRHKAKVYPEKHRYCADNSFLHNDVDVPSILEKAFSTLPTRKSLVLYN
SLIPTSRRDLPPMALSVQSDHYFALYGIWEDAKDDVHNQAWVSNIMEEVGRHSTGAYIGE
FDFLKRQSRLWGFQEKEKLKAIRQKWDPNGVFCSYLGLELGL

Enzyme Prediction     

No EC number prediction in TSTA_061230-t26_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	40	454	3.6e-68	0.982532751091703

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	1.25e-20	51	186	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	2.23e-19	46	452	27	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AHG26149.1|AA7	1.15e-24	21	219	17	213
QRD00400.1|AA7	1.95e-24	29	229	26	225
CAK49173.1|AA7	3.28e-24	19	240	27	242
QUC19098.1|AA7	4.37e-24	51	219	48	218
CDR44461.1|AA7	4.96e-23	45	229	64	249

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	2.67e-29	21	452	15	453	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	6.74e-29	21	452	15	453	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	6.74e-29	21	452	15	453	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	9.18e-29	21	452	15	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYB_A	9.18e-29	21	452	15	453	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|A0A0E3D8N0|JANO_PENJA	3.66e-99	14	449	2	436	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	7.09e-99	18	449	7	437	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	5.02e-90	20	456	9	442	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	7.08e-90	20	456	9	442	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|Q796Y5|YGAK_BACSU	1.82e-23	33	452	18	436	Uncharacterized FAD-linked oxidoreductase YgaK OS=Bacillus subtilis (strain 168) OX=224308 GN=ygaK PE=3 SV=4

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000038	0.000000

TMHMM  Annotations     

There is no transmembrane helices in TSTA_061230-t26_1-p1.