CAZyme Information: FGRAMPH1_01T13301-p1

Basic Information

• Species: Fusarium graminearum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium graminearum
• CAZyme ID: FGRAMPH1_01T13301-p1
• CAZy Family: GH16
• CAZyme Description: 6-hydroxy-d-nicotine oxidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1247	HG970333|CGC16	137151.28	6.4132

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FgraminearumPH-1	14145	229533	2	14143

• Gene Location: location=HG970333:5614975-5618718(+)

Full Sequence      

MTWHAQLVLVLALVCLVNASCSGRSDACSSNPILVRRVNTLNFQPESCNLKWKLGCTRPD
KNGGKEQKPPPYPLCTTWDYPSGLLPVDSYTLSLQANTFSKGSANATLHGLWPGSVGGKG
AKNQPYGCRNGEEFDETIPKTFHDLLKYFWPTNPEFKNTMQCFILSEWMKHGTCAVIPGA
DGEAFRLSQESYFRTAFVLANEFNANIALQEQLKAPTPMTDMEPLITTRCVQCAYLATVG
WEGTDVASVPRMSADCIDTCFACGKDWDRCPPAQLESTVELDPSNAPPNESGSGSDGPAS
FRSLDFAVPGLVNSENISPWEGTWRSFGAEQLGSGKFEFAQTFTDTTMTVTTDSPYPQTC
NYERRGPGELVLKCGSNNSHLEECLVQRLPDVGGLEAAFLACNHTGAPAPGSFFTAMDTP
GCGNFLMFRCKASAAGCSFSPDVVSADDSKATKPNAGAESDSKPSYISHSHPGIAGSPLK
LLGTWRTLQVSSHYEKGLARWNFTSDGQASMEWPNYPSRGVTRYSVSHSQEDPSRVLLAD
ATGAITNCRFRFQYQPVYSYATLDCDAPDQQAGDKKSSQHTKWAMGRCNPCSASCRYSCG
PENDMCGVGSCDPAESTETEHAGASLPAKDGHNWCTPEDSSCWPTKTAILNLEQALDPTV
PRLGLQWNNYPQPQPAPVPMGSIKNQSFYGLGSQGLKALYYYEDINEMQRPCYSASGDVK
IWNDVSDMCKAALHQNEYRDWNPFIVVFPLNERHVAAALTFAAQHRLCIATAGTGHEYNS
RNSCPTGGILIRTILLKDKTFIPTWNQDPTIAPAGAFRFGAGSIFAEMHAYSAKYDRVVA
SGWCSTVGMVGFHLGGGHGPFAPSMGLGVDNLLEIEVLQVGSDAQDNPVVHKKIASRQEN
PQLFWAMRGGGGGVWGVILSMTIRAHEVPDGGLNRVFISQKGNFCPGPRDFGYEWLRDMW
VRFAAWQLKLNHKVSTQPAFFINTTDYKNGDLCKVTWSFNFEYFYAGGQKEEDYKLFRDG
LQHVLKNYTAQEDRYESAYEYLLSMPANKFSLISTNPLPASSPPSDAATGSQNSVLVSRQ
MMETKFASTMMDVLDICVKTLKSPDKTSPDPAGYRCGFHYLYTSLTGNLGSVQPKDTAIS
TGFRSALMLWNARTLTTQQANETIYKLGPNSYFSESSYVMHNWTTRYWGEKKYGQLLAVK
KAHDPKNLFWCHHCVGDNPKDAYGEPLGPQGDVVKEKKPKVEVKDEL

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	733	930	2.5e-40	0.39082969432314413

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.24e-14	743	878	1	129	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.
238220	RNase_T2	1.48e-11	88	204	2	115	Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen.
238512	RNase_T2_euk	1.32e-10	88	212	12	124	Ribonuclease T2 (RNase T2) is a widespread family of secreted RNases found in every organism examined thus far. This family includes RNase Rh, RNase MC1, RNase LE, and self-incompatibility RNases (S-RNases). Plant T2 RNases are expressed during leaf senescence in order to scavenge phosphate from ribonucleotides. They are also expressed in response to wounding or pathogen invasion. S-RNases are thought to prevent self-fertilization by acting as selective cytotoxins of "self" pollen. Generally, RNases have two distinct binding sites: the primary site (B1 site) and the subsite (B2 site), for nucleotides located at the 5'- and 3'- terminal ends of the sessil bond, respectively. This CD includes the eukaryotic RNase T2 family members.
395357	Ribonuclease_T2	3.84e-10	107	211	32	124	Ribonuclease T2 family.
223354	GlcD	2.25e-09	738	877	28	159	FAD/FMN-containing dehydrogenase [Energy production and conversion].

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QKD57322.1|GH43_11	1.20e-16	743	929	598	775
QKD57322.1|CBM91|GH43_11	1.20e-16	743	929	598	775
QUC19098.1|AA7	1.80e-09	743	971	48	248
UQC87672.1|AA7	4.43e-09	706	929	33	238
UNI23960.1|AA7	9.58e-09	743	929	48	218

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6F72_A	5.13e-19	676	927	56	298	Crystal structure of VAO-type flavoprotein MtVAO615 at pH 7.5 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_A Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],6F73_B Crystal structure of VAO-type flavoprotein MtVAO615 at pH 5.0 from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464]
6FYE_A	7.33e-14	721	928	23	211	The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
6FYD_A	1.70e-13	721	928	23	211	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]
6FYF_A	2.99e-13	721	928	23	211	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	3.95e-13	721	928	23	211	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|L0E159|MALF_MALAU	4.76e-22	635	925	27	300	FAD-linked oxidoreductase malF OS=Malbranchea aurantiaca OX=78605 GN=malF PE=1 SV=1
sp|A0A7L8UYL4|FFSJ_ASPFV	5.32e-22	755	1216	135	587	FAD-linked oxidoreductase ffsJ OS=Aspergillus flavipes OX=41900 GN=ffsJ PE=3 SV=1
sp|L0E2Q5|PHQH_PENFE	2.05e-21	755	926	131	299	FAD-linked oxidoreductase phqH OS=Penicillium fellutanum OX=70095 GN=phqH PE=3 SV=1
sp|D4B1Z7|A2478_ARTBC	1.63e-20	743	1216	122	558	Uncharacterized FAD-linked oxidoreductase ARB_02478 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_02478 PE=1 SV=1
sp|A0A0A2KMZ4|CNSA_PENEN	1.91e-20	754	929	31	201	Aurantioclavine synthase cnsA OS=Penicillium expansum OX=27334 GN=cnsA PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	CS Position
0.000202	0.999750	CS pos: 19-20. Pr: 0.9820

TMHMM  Annotations     

There is no transmembrane helices in FGRAMPH1_01T13301-p1.