CAZyme Information: EEU42004.1

Basic Information

• Species: Fusarium vanettenii
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium vanettenii
• CAZyme ID: EEU42004.1
• CAZy Family: GH43
• CAZyme Description: FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:C7Z1H0]

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
483		53801.09	5.8772

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Fvanettenii77134	15708	660122	0	15708

• Gene Location: location=GG698906:1016581-1018145(+)

Full Sequence      

MTSSASPDVILPTVLQRGTSDYENSRERYFNKEETDRFPIEIHAVQSVEDVYKALQRAQE
LGVAVGVRSGGHLPSKPSLINNGILIDVSHLNREIKYDSQTGQVSFGPAVRVYEAWKSTD
ALGRFFPFGHAPDVALGGFCLAGGQGFFMRGWGATVTDWIIKLEIVVPDGRVLIASKTEN
SDLFWAARGAGQAFFGVVTRIWSRTIPKKKHYGRAYTFSGKDNYEAFLSFAFERNNQMPK
SFTETAACTLHPELFEPDSPDESVPSTSPLLLLVNISAYADTLSEAESMLSVWDQVPENL
KGCLIESKPVAEVDWEEFFKLQHLLNPQTPGQKWGINSILNDPAIPRDKLIEAIKPAMCN
LPTRSSYGCIYMADTLDVDEADAVLSIPQQYYISTFSGWKDVSLQTKVRQVMQHSYKQAE
SVACGMYVADFDQSPGALHSSSIPVWSKSACAKFMRIREKWDPKGLFIGYKAFVLTPKED
TKL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	27	256	1.6e-58	0.49563318777292575

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.85e-21	44	176	6	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	5.43e-21	42	355	35	350	FAD/FMN-containing dehydrogenase [Energy production and conversion].
273751	FAD_lactone_ox	8.64e-07	47	188	23	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.
178402	PLN02805	1.40e-05	19	208	111	309	D-lactate dehydrogenase [cytochrome]
273750	pln_FAD_oxido	7.26e-05	49	223	42	223	plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UNI23960.1|AA7	2.44e-19	39	207	48	216
UPK90596.1|AA7	5.04e-19	36	208	14	189
QUC19098.1|AA7	2.50e-18	39	211	48	220
CAI94231.1|AA7|1.1.3.-	4.68e-18	18	210	40	231
AHG26149.1|AA7	1.59e-17	39	208	42	212

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6FYD_A	5.95e-21	20	199	28	202	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	1.44e-20	20	199	28	202	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	1.44e-20	20	199	28	202	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	1.93e-20	20	199	28	202	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	1.93e-20	20	199	28	202	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|A0A2I6PJ02|NODO_HYPPI	1.28e-36	19	469	19	442	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A0E3D8N0|JANO_PENJA	1.21e-35	20	469	17	441	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	1.45e-30	15	463	12	433	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	6.86e-30	15	207	12	202	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A5ABH0|PYNB_ASPNC	1.41e-18	28	198	64	232	FAD-linked oxidoreductase pynB OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=pynB PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000089	0.000000

TMHMM  Annotations     

There is no transmembrane helices in EEU42004.1.