CAZyme Information: PPTG_19661-t26_1-p1

Basic Information

• Species: Phytophthora parasitica
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora parasitica
• CAZyme ID: PPTG_19661-t26_1-p1
• CAZy Family: GT76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
509		54820.07	9.0773

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PparasiticaINRA-310	23240	761204	119	23121

• Gene Location: location=KI669717:426-1955(+)

Full Sequence      

MVASVSGASRAIIALCSVIAAHGGFAVAAGTQADVGSCLNKAGIENSVPTTTTWTMDIQP
WNSRVNPVPAAVAFPKTEKEVSAALKCAASAGVKVTTLGGNRSFSSMGFGRNDGALVINL
KALKHLKYDPSTKLLSYGGPVMISEAANHMWNKYKRTLPHGRCPDVGMTGVAASGFGTLS
RSSGTVLDNIESVRVALANGTIVDADAKRNSHVYWGVRGAASSMGVVLDFKIKTLDPPSE
RVTNYTIAFNSSYKPTQQDNVDALIGTQTWALSKDNNDLVSIRFSLKTKSTLQGFFYGGG
AKAKAVLGSLMKNLPPSMVLTSNENDFWTSEDISTPGLQKETLTPRRYFYIASVTIPRST
PLDNATAWELFSGTAFAPKLPDASASGFVDIWGGAYAKTVKADTSAWKHDDNLHLVRWDM
RTASFDVKFADSSITTMREHFYKFVDAYKASGGVPGGFTTYRDERWTVPEMAEYLYGGGN
FERLQKIKTEVDPNEMFNTDPQAIPALTA

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	59	287	1.4e-48	0.48034934497816595

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.36e-21	69	206	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.
223354	GlcD	1.77e-18	62	498	25	451	FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402	PLN02805	3.19e-07	59	267	122	331	D-lactate dehydrogenase [cytochrome]
369658	BBE	3.45e-07	461	505	5	45	Berberine and berberine like. This domain is found in the berberine bridge and berberine bridge- like enzymes which are involved in the biosynthesis of numerous isoquinoline alkaloids. They catalyze the transformation of the N-methyl group of (S)-reticuline into the C-8 berberine bridge carbon of (S)-scoulerine.
273751	FAD_lactone_ox	2.64e-06	59	233	5	177	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
UPT50362.1|AA7	3.40e-304	1	507	1	504
UIZ28076.1|AA7	3.45e-268	1	507	1	535
UQC82098.1|AA7	2.21e-86	19	505	7	492
CEI61048.1|AA7	2.26e-76	27	505	21	497
QPC70090.1|AA7	8.77e-76	27	505	21	497

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YJI_A	2.11e-78	27	505	1	477	Chain A, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1],6YJI_B Chain B, FAD-binding PCMH-type domain-containing protein [Fusarium graminearum PH-1]
3RJ8_A	1.24e-45	37	504	5	469	Crystal structure of carbohydrate oxidase from Microdochium nivale [Microdochium nivale],3RJA_A Crystal structure of carbohydrate oxidase from Microdochium nivale in complex with substrate analogue [Microdochium nivale]
5K8E_A	1.32e-44	32	504	24	492	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]
1ZR6_A	4.49e-41	35	497	9	470	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]
3HSU_A	7.91e-40	35	497	9	470	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
sp|I1SB12|MNCO_MICNN	2.58e-45	31	504	21	491	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
sp|G2QG48|XYLO_MYCTT	6.80e-44	32	504	24	492	Xylooligosaccharide oxidase OS=Myceliophthora thermophila (strain ATCC 42464 / BCRC 31852 / DSM 1799) OX=573729 GN=xylO PE=1 SV=1
sp|E9F5F1|SUBF_METRA	1.34e-40	37	506	31	491	FAD-linked oxidoreductase subF OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=subF PE=3 SV=1
sp|Q6PW77|GOOX_SARSR	2.17e-40	35	497	28	489	Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
sp|I1S2K2|CHITO_GIBZE	8.31e-38	35	504	27	488	Chitooligosaccharide oxidase OS=Gibberella zeae (strain ATCC MYA-4620 / CBS 123657 / FGSC 9075 / NRRL 31084 / PH-1) OX=229533 GN=chitO PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
0.610560	0.389434

TMHMM  Annotations     

There is no transmembrane helices in PPTG_19661-t26_1-p1.