CAZyme Information: FOIG_09339-t36_1-p1

Basic Information

• Species: Fusarium odoratissimum
• Lineage: Ascomycota; Sordariomycetes; ; Nectriaceae; Fusarium; Fusarium odoratissimum
• CAZyme ID: FOIG_09339-t36_1-p1
• CAZy Family: GH18
• CAZyme Description: unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
466		50820.81	5.0203

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_FodoratissimumNRRL54006	16975	1089451	341	16634

• Gene Location: location=JH658286.1:379650-381050(+)

Full Sequence      

MSAQIKGIESLQCEYVVPDNDTPQLPRWSDTHIQRPALIVTPKTEEDVKDAIRVANENKL
IIVAAGGGHGTFVSVDPASLYLDMKLFKKIALNKDEGTVKVGGGVIVGEVLKTLADEGYY
TPIPNSDAVGFVGSMLGGGNSAQIGLHGWMVDNMVSFRLITASGDIVEVDSSSKDKEQSL
FNVLCGAGHGLGVVTELTVSAFPLSSLNMEDNKIWTRSLIFPAPALDIAINAFLDLSHPP
AEGYMSLAFARSPPGTPAAGSPIIILGYQYFGPAEQAEKATTLLFQDDVVSKTVVANTEL
LPFENVNAKMNIYNSHHGHKTIASCRLHKTTAEAIKAGFEKWRIATEDYPDAQQSSLIIS
AYNIDKTSAIKNEKFVEGRDRNINAFMVMVAKEDKTREAFGPILDDVVAGFRKSDEGMVP
RSFPNNLRPGKDLSEMYDTERLEVLRDVKKTWDADGVFWSPYFKAV

Enzyme Prediction     

EC	1.1.3.-:1

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	27	206	1e-37	0.388646288209607

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	1.47e-19	34	299	30	309	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	7.80e-14	36	170	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.
178402	PLN02805	3.16e-09	36	199	134	302	D-lactate dehydrogenase [cytochrome]
273751	FAD_lactone_ox	6.59e-07	24	203	3	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.
215258	PLN02465	5.08e-05	19	203	80	262	L-galactono-1,4-lactone dehydrogenase

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
UDD62121.1|AA7	1.83e-12	36	208	41	218
QRD93627.1|AA7	9.77e-12	36	210	48	222
QMW46638.1|AA7	9.77e-12	36	210	48	222
UDD63515.1|AA7	9.77e-12	36	210	48	222
QRC92907.1|AA7	2.39e-11	35	209	62	237

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
2BVF_A	2.08e-21	1	237	2	238	Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVF_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 3 (P1) [Paenarthrobacter nicotinovorans],2BVG_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVG_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 1 (P21) [Paenarthrobacter nicotinovorans],2BVH_A Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_B Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_C Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans],2BVH_D Crystal structure of 6-hydoxy-D-nicotine oxidase from Arthrobacter nicotinovorans. Crystal Form 2 (P21) [Paenarthrobacter nicotinovorans]
6FYD_A	1.80e-12	28	195	37	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]
3HSU_A	7.42e-10	36	202	43	209	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1ZR6_A	9.83e-10	36	202	43	209	The crystal structure of an Acremonium strictum glucooligosaccharide oxidase reveals a novel flavinylation [Sarocladium strictum],2AXR_A Crystal structure of glucooligosaccharide oxidase from Acremonium strictum: a novel flavinylation of 6-S-cysteinyl, 8alpha-N1-histidyl FAD [Sarocladium strictum]
4EC3_A	8.97e-08	24	204	40	222	Structure of berberine bridge enzyme, H174A variant in complex with (S)-reticuline [Eschscholzia californica]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|A0A1J0KJK5|IACH_PESFW	2.69e-24	27	458	73	501	FAD-linked oxidoreductase iacH OS=Pestalotiopsis fici (strain W106-1 / CGMCC3.15140) OX=1229662 GN=iacH PE=1 SV=1
sp|Q7SHH8|SRDI_NEUCR	3.36e-24	40	458	78	489	FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1
sp|Q0CF74|AZPB3_ASPTN	9.76e-24	8	198	27	225	FAD-linked oxidoreductase ATEG_07660 OS=Aspergillus terreus (strain NIH 2624 / FGSC A1156) OX=341663 GN=ATEG_07660 PE=1 SV=1
sp|G4N285|OXR1_MAGO7	1.16e-23	40	458	82	496	FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1
sp|G9N4A7|VIRF_HYPVG	2.10e-22	27	458	20	444	FAD-linked oxidoreductase virF (Fragment) OS=Hypocrea virens (strain Gv29-8 / FGSC 10586) OX=413071 GN=virF PE=3 SV=1

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 FOIG_09339-t36_1-p1.