CAZyme Information: PHYSODRAFT_320903-t26_1-p1

Basic Information

• Species: Phytophthora sojae
• Lineage: Oomycota; NA; ; Peronosporaceae; Phytophthora; Phytophthora sojae
• CAZyme ID: PHYSODRAFT_320903-t26_1-p1
• CAZy Family: GH1
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
504		54274.79	9.8659

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_PsojaeP6497	28142	1094619	1653	26489

• Gene Location: location=JH159151:1907974-1909488(+)

Full Sequence      

MVSSASSAIFALCSLIAAQSGLASAAATPVDLGSCLTKAGIENSVPRTTTWTMDIQPWNS
RINPQPAAVAFPKTEAQVSAALKCAGSAGVKVTTLGGNRSFSSMGFGRNNGALVMNLKHM
KHLKYDASTGLLSYGGPVMISETAKYMWGFKRTLPHGRCPDVGMTGVAASGFGTLSRAAG
TVLDNIEAVRVALANGSIVDASAKQNSDLFWGVRGAASSMGVVLDFKIKTMAPPSQTVTN
YTIAFDKSAKPTQQDNVNAFIGTQKWALSADNNDLLSIRFSLKTKSTLQGFFYGSSAQAK
TVFASLMKNLPPSMVLTTTEEDFWTSETYSTPGLIEQTMSPRRYFYIASVTIPSNKPLTN
ATAWDLFSSTAYAPALPDASASGFVDIWGGRYAKGVKADASAWKHDDRLHLIRWDIRTPS
FDVKFADSTITTMRSNFYKFVSSYKASGGVPGGFTTYRDERWTIKEMAEYLYGGGNFAKL
QQIKTKYDPKMMFNTDPQAIPALA

Enzyme Prediction     

EC	1.1.3.-:2

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
AA7	56	495	3.3e-57	0.980349344978166

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
396238	FAD_binding_4	3.67e-21	66	202	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	4.11e-21	58	239	23	212	FAD/FMN-containing dehydrogenase [Energy production and conversion].
178402	PLN02805	9.78e-07	66	339	134	382	D-lactate dehydrogenase [cytochrome]
369658	BBE	2.45e-06	457	501	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	2.61e-05	56	229	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	5.72e-290	2	504	5	505
UIZ28076.1|AA7	1.52e-251	2	503	5	535
UQC82098.1|AA7	6.26e-88	32	501	24	492
UQC77503.1|AA7	9.56e-75	11	501	11	503
CEI61048.1|AA7	1.86e-72	32	501	30	497

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6YJI_A	3.70e-73	32	501	10	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	6.07e-48	34	500	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]
6Y0R_AAA	2.03e-43	32	500	27	488	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
1ZR6_A	2.43e-43	31	493	8	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	4.38e-42	31	493	8	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	3.41e-47	23	500	16	491	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
sp|I1S2K2|CHITO_GIBZE	1.04e-42	32	500	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
sp|Q6PW77|GOOX_SARSR	1.17e-42	31	493	27	489	Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
sp|E9F5F1|SUBF_METRA	1.80e-41	34	504	31	493	FAD-linked oxidoreductase subF OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=subF PE=3 SV=1
sp|G2QG48|XYLO_MYCTT	7.40e-41	15	500	6	492	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 SP

Other	SP_Sec_SPI	CS Position
0.000252	0.999717	CS pos: 25-26. Pr: 0.9700

TMHMM  Annotations     

There is no transmembrane helices in PHYSODRAFT_320903-t26_1-p1.