CAZyme Information: FOMG_11474-t38_1-p1

Basic Information

• Species: Fusarium oxysporum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium oxysporum
• CAZyme ID: FOMG_11474-t38_1-p1
• CAZy Family: GH30
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
472		52953.58	6.6041

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Foxysporum26406	20033	1089452	372	19661

• Gene Location: location=JH659337.1:172426-174025(-)

Full Sequence      

MTQIDALAQAKSQLPPSFPIIWRGDVSWERARVGRVFNHRRPSSQPLAVVEATREDHIVE
AVRLARTLGARVSVRSGGHSWAAWSVREGAVLIDLGKYHEFLLDDSTGVLQASPSMTGRM
VNKLLGLRGRMFPGGHCPEVALGGFLLQGGMGWNCKNWGFACERLMALDVVTADGEKRHC
DKTTNTELYWAARGSGPGFPAVVTRFYLQTIPVFNHMRSSVYIYEKKDYEAAFSWVLKLA
PTFDEGTEIVAVGQHLPGREGEHILISFVTFKNSDEEARSALQPAQDSAPPGHVDSWFCK
TTSLAEQYDHQHSANPEGHRYAVDNSYIRNDADVVSVLKESFTSLPTKKSFTLWYAMAPG
SRRSIEDDNFEDMALSMQTDHYYAAYVIWEDQADDLKCQSWLTHVFDKIKRDSEGSYLGD
ADFQKRLAVFWGQDQGKRLMNIRKKWDPQGVVAGYLNKGDQNGVEGLENVHN

Enzyme Prediction     

No EC number prediction in FOMG_11474-t38_1-p1.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	34	451	2.6e-71	0.9781659388646288

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	2.57e-27	46	181	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	1.58e-25	30	259	16	250	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	5.13e-07	43	215	12	183	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
UPK90596.1|AA7	5.36e-24	46	453	20	436
BAI44126.1|AA7|CBM18	9.64e-24	19	210	251	440
QBZ61916.1|AA7|CBM18	9.64e-24	19	210	251	440
ATZ50592.1|AA7	5.66e-23	46	211	70	237
CCD53507.1|AA7|CBM18	1.07e-22	41	210	72	243

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	8.65e-23	20	448	22	449	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]
3RJ8_A	1.67e-22	37	448	29	459	Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
6FYF_A	2.11e-22	20	448	22	449	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	2.11e-22	20	448	22	449	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]
6FYB_A	2.84e-22	20	448	22	449	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	9.02e-103	16	456	4	443	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	1.24e-102	17	456	8	444	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	1.29e-96	11	448	2	433	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	1.43e-95	11	448	2	433	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|I1SB12|MNCO_MICNN	9.81e-22	37	448	51	481	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000064	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FOMG_11474-t38_1-p1.