CAZyme Information: FPRN_01917-t42_1-p1

Basic Information

• Species: Fusarium proliferatum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium proliferatum
• CAZyme ID: FPRN_01917-t42_1-p1
• CAZy Family: AA4
• CAZyme Description: related to 6-hydroxy-D-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
442		49026.61	5.3239

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FproliferatumNRRL62905	15602	N/A	348	15254

• Gene Location: location=FCQG01000001:1860161-1861587(+)

Full Sequence      

MASLPKILSQKSEGYEQTRLKFFNGRVPDIHPTEIAIPSTTAEVVSAVKRARENGWKVGV
RSGGHLFFCNALLEGGLLIDTRNLNKDVGYDAATNIATISPGHRVEDVTTFLKARGRFFP
SGHSRSVAVGGFLLAGGQGCFMRGWGYTAPTWVTQLEVVTSEGETVIANKAQNSDLFWAA
PGSGQGFFGVVTRIWVKTIPTRNLFDKTVIVDSTDIFKPLLKWTLEMSRKVPKYGVDLFY
CTFFADKDDPNGGHESAAKRIFFAINLTIFADSLDEAAVLASPLETFPEDFKKYIVTTVP
LVERTWDELWALQESFQPQGNGERWNVDSILVDPKASDDELIDAITPALYDLPSRLSSGT
FCPMDYYPDEADQALSLPQKAYVSTMCCWKDPKHDAAVDKWLLDAYTKADQVSCGVYVAD
FNMKHRKPRYTGHDGLCPEEVA

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	23	232	9.4e-58	0.4519650655021834

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	5.34e-29	14	361	14	368	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	1.13e-25	32	169	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	1.23e-09	6	218	9	198	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.
273750	pln_FAD_oxido	3.83e-09	29	215	29	222	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.
215242	PLN02441	1.41e-07	153	193	194	233	cytokinin dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UPK90596.1|AA7	7.06e-24	30	203	18	191
QRD93627.1|AA7	5.01e-21	15	203	32	218
UDD63515.1|AA7	5.01e-21	15	203	32	218
EGX49222.1|AA7|CBM1	1.08e-20	21	229	154	352
QMW46638.1|AA7	1.65e-20	15	203	32	218

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5I1V_A	1.82e-16	32	198	31	204	Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1V_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_A Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_B Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_C Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6],5I1W_D Crystal structure of CrmK, a flavoenzyme involved in the shunt product recycling mechanism in caerulomycin biosynthesis [Actinoalloteichus sp. WH1-2216-6]
3VTE_A	2.53e-15	20	289	44	307	Crystal structure of tetrahydrocannabinolic acid synthase from Cannabis sativa [Cannabis sativa]
2WDW_A	4.54e-15	5	197	40	230	The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],2WDW_B The Native Crystal Structure of the Primary Hexose Oxidase (Dbv29) in Antibiotic A40926 Biosynthesis [Nonomuraea gerenzanensis],5AWV_A Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_B Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_C Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis],5AWV_D Crystal structure of glycopeptide hexose oxidase DBV29 complexed with teicoplanin [Nonomuraea gerenzanensis]
2Y08_A	6.14e-15	32	198	59	232	Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y08_B Structure of the substrate-free FAD-dependent tirandamycin oxidase TamL [Streptomyces sp. 307-9],2Y3R_A Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_B Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_C Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3R_D Structure of the tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P21 space group [Streptomyces sp. 307-9],2Y3S_A Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y3S_B Structure of the tirandamycine-bound FAD-dependent tirandamycin oxidase TamL in C2 space group [Streptomyces sp. 307-9],2Y4G_A Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9],2Y4G_B Structure of the Tirandamycin-bound FAD-dependent tirandamycin oxidase TamL in P212121 space group [Streptomyces sp. 307-9]
6EO5_A	1.28e-14	32	231	48	253	Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens],6EO5_B Physcomitrella patens BBE-like 1 variant D396N [Physcomitrium patens]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A0E3D8N0|JANO_PENJA	1.41e-46	15	430	19	417	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	2.70e-45	9	430	16	418	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	3.12e-31	8	430	12	415	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	3.12e-31	8	227	12	229	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|O06997|YVDP_BACSU	1.66e-18	6	197	9	197	Uncharacterized FAD-linked oxidoreductase YvdP OS=Bacillus subtilis (strain 168) OX=224308 GN=yvdP PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000046	0.000000

TMHMM  Annotations     

There is no transmembrane helices in FPRN_01917-t42_1-p1.