CAZyme Information: PMAA_101920-t26_2-p1

Basic Information

• Species: Talaromyces marneffei
• Lineage: Ascomycota; Eurotiomycetes; ; Trichocomaceae; Talaromyces; Talaromyces marneffei
• CAZyme ID: PMAA_101920-t26_2-p1
• CAZy Family: GT4
• CAZyme Description: FAD binding oxidoreductase, putative

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
458		51236.64	5.8438

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_TmarneffeiATCC18224	10194	441960	145	10049

• Gene Location: location=DS995902:3203765-3205308(+)

Full Sequence      

MWLPSFGFFKESEPPLSIVWRGRENETLYENARVKRVFNCQRPRRYPRAVVSAKAQSDVV
KAVKLATDQRCSVSVRAGGHSWPVWSLRDDTILIDLGNFSKISFDEETGVVKASPSTTSE
ELTEYLHPKGRIFPTGHCPDVGIGGYLLCGGMGWNSNSWGWACEHVVAVDVVTSSGEVVR
ADAKQNSDLLWAARGAGPGFPGLVTDFHLQTRPLPKAMRSSLYIYKMSYYQNVFDWALKI
SSGVDEGLQIAVVGSYPSGFDEPCITVALLALGDSDESVTEVLRLADESHPEGTAVRSYC
DETSLKEQFRHKRGAYPEGHRYCADNSFLNNDADVGSVLKSAFSTLPTRKSLALYNSMIP
TSRRQLPSMALSVQSDHYFALYGIWEDENDDALNQAWVSDIMKQVGKHSVGAYTGEFDFQ
MRRSRFWGDEQKEKLKNIREKWDPNGIFCDYLGLEVDL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	35	448	1.7e-75	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	4.13e-35	42	448	27	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	8.70e-31	47	182	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.
273751	FAD_lactone_ox	3.30e-05	54	213	22	180	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.
178402	PLN02805	2.33e-04	47	216	134	309	D-lactate dehydrogenase [cytochrome]

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QRD00400.1|AA7	1.59e-29	24	215	25	217
QUC19098.1|AA7	3.12e-28	47	215	48	218
BAI44126.1|AA7|CBM18	8.94e-28	47	218	275	447
QBZ61916.1|AA7|CBM18	8.94e-28	47	218	275	447
AHG26149.1|AA7	2.47e-27	47	215	42	213

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	1.89e-27	18	448	22	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	4.75e-27	18	448	22	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	4.75e-27	18	448	22	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]
6FYB_A	6.45e-27	18	448	22	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]
6FYE_A	6.45e-27	18	448	22	453	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0E3D8N0|JANO_PENJA	1.02e-106	14	444	4	435	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	1.98e-103	12	445	5	437	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	8.14e-94	16	444	9	433	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	1.28e-92	16	444	9	433	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|P08159|HDNO_PAENI	1.37e-23	47	319	38	308	(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2

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 PMAA_101920-t26_2-p1.