CAZyme Information: jhhlp_004851-t41_1-p1

Basic Information

• Species: Lomentospora prolificans
• Lineage: Ascomycota; Sordariomycetes; ; Microascaceae; Lomentospora; Lomentospora prolificans
• CAZyme ID: jhhlp_004851-t41_1-p1
• CAZy Family: GH16
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
466	NLAX01000095|CGC1	52160.62	5.1511

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_LprolificansJHH5317	8768	N/A	208	8560

• Gene Location: location=NLAX01000095:66265-67852(+)

Full Sequence      

MIPPNEVGRPALPIIYRDTSDSNTFRNAAWGRVFNERRDYSRRPKAVVLASTSEHVKAAV
LLANEQNCRVSVRSGGHSWAAWSVRDEAILIDLGDLKGVSYDEETKIVTCTPSSTGRIVN
GLLKEKGRMFAGGHCPDVGLGGFLLQGGMGWNCKNWGWACENIARIEVVTAKGEELECSE
TENSDLFWAARGAGPGFPAVITKFHLRTRPLFSLFDSTYIYPVSRYREVLQWVVDVSPTA
DSDMEIVCVSRCNPDTGEIEIVAGFTVFKATQEEAEAALTPINQSRPKDPAVEVFCLQNS
LEWQYKNQAAANPENHRYCCENSYVANDADVPAVLEAAFTTLPSKKAFALYFAMNPTSRR
PLPDMALSMQSDHYFALYTVWEDAADDQPCTTWVHDVMRDVERHSVGSYLGDADFQHRRT
KYWSDESGKKLMEIRKKWDPQGRICGYLDAGDKSGVEGLKNEYEWS

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	37	442	8.9e-79	0.9650655021834061

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	8.95e-25	37	443	25	449	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	7.11e-21	44	179	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.
215242	PLN02441	2.95e-06	162	203	193	233	cytokinin dehydrogenase
273751	FAD_lactone_ox	3.61e-06	40	231	11	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.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
BAI44126.1|AA7|CBM18	4.42e-31	12	208	250	440
QBZ61916.1|AA7|CBM18	4.42e-31	12	208	250	440
ANF89368.1|AA7	7.12e-29	34	208	53	227
AEO58513.1|AA7|1.1.3.-	7.12e-29	34	208	53	227
AEO62186.1|AA7	2.02e-27	18	208	37	225

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5K8E_A	2.46e-30	34	208	53	227	Xylooligosaccharide oxidase from Myceliophthora thermophila C1 [Thermothelomyces thermophilus ATCC 42464],5L6F_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylobiose [Thermothelomyces thermophilus ATCC 42464],5L6G_A Xylooligosaccharide oxidase from Myceliophthora thermophila C1 in complex with Xylose [Thermothelomyces thermophilus ATCC 42464]
6FYD_A	5.21e-29	32	440	35	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]
6FYF_A	1.32e-28	32	440	35	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	1.32e-28	32	440	35	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]
6FYE_A	1.79e-28	32	440	35	449	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|A0A0E3D8N0|JANO_PENJA	2.35e-104	10	450	4	445	FAD-linked oxidoreductase janO OS=Penicillium janthinellum OX=5079 GN=janO PE=3 SV=1
sp|A0A0E3D8N6|PENO_PENCR	9.66e-104	11	453	8	447	FAD-linked oxidoreductase penO OS=Penicillium crustosum OX=36656 GN=penO PE=3 SV=1
sp|A0A140JWT7|PTMO_PENSI	3.85e-103	12	453	9	447	FAD-linked oxidoreductase ptmO OS=Penicillium simplicissimum OX=69488 GN=ptmO PE=3 SV=1
sp|A0A2I6PJ02|NODO_HYPPI	7.19e-100	12	448	9	444	FAD-linked oxidoreductase nodO OS=Hypoxylon pulicicidum OX=1243767 GN=nodO PE=3 SV=1
sp|G2QG48|XYLO_MYCTT	1.26e-29	34	208	53	227	Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000059	0.000000

TMHMM  Annotations     

There is no transmembrane helices in jhhlp_004851-t41_1-p1.