dbCAN-seq: a database of CAZyme sequence and annotation

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CAZyme Information: POW11835.1

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Basic Information help

Species

Puccinia striiformis

Lineage

Basidiomycota; Pucciniomycetes; ; Pucciniaceae; Puccinia; Puccinia striiformis

CAZyme ID

POW11835.1

CAZy Family

GH27

CAZyme Description

unspecified product

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
1065		117147.63	7.1337

Genome Property

Genome Version/Assembly ID	Genes	Strain NCBI Taxon ID	Non Protein Coding Genes	Protein Coding Genes
FungiDB-61_Pstriiformis93TX-2	14629	N/A	0	14629

Gene Location

Full Sequence Download help

Enzyme Prediction help

EC	1.1.3.-:1	1.1.3.-:1

CAZyme Signature Domains help

Family	Start	End	Evalue	family coverage
AA7	575	1020	8.9e-91	0.9934497816593887
AA7	71	526	6.5e-86	0.9847161572052402

CDD Domains download full data without filtering help

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
223354	GlcD	3.55e-22	51	289	4	246	FAD/FMN-containing dehydrogenase [Energy production and conversion].
223354	GlcD	9.08e-22	560	1014	6	450	FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238	FAD_binding_4	3.13e-20	80	217	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.
396238	FAD_binding_4	5.50e-20	587	724	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.
369658	BBE	2.12e-11	975	1020	1	44	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.

CAZyme Hits help

Hit ID	E-Value	Query Start	Query End	Hit Start
3.86e-112	567	1020	46	490
1.53e-109	567	1020	45	489
1.53e-109	567	1020	45	489
1.17e-107	567	1020	45	489
9.10e-100	558	1021	246	717

PDB Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
4.61e-87	41	541	4	495	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]
8.61e-86	41	541	4	495	Chain A, Glucooligosaccharide oxidase [Sarocladium strictum]
1.02e-80	568	1020	42	488	Chain AAA, Chitooligosaccharide oxidase [Fusarium graminearum PH-1]
6.84e-77	558	1020	8	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]
2.16e-74	69	527	50	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]

Swiss-Prot Hits download full data without filtering help

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
5.49e-85	70	527	52	498	Glucooligosaccharide oxidase OS=Sarocladium strictum OX=5046 GN=gluO PE=1 SV=1
5.23e-80	568	1020	42	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
6.35e-76	558	1020	30	491	Carbohydrate oxidase OS=Microdochium nivale OX=5520 GN=MnCO PE=1 SV=2
4.24e-74	557	1020	29	489	FAD-linked oxidoreductase subF OS=Metarhizium robertsii (strain ARSEF 23 / ATCC MYA-3075) OX=655844 GN=subF PE=3 SV=1
1.11e-73	69	527	50	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 help

This protein is predicted as OTHER

Other	SP_Sec_SPI	CS Position
1.000044	0.000000

TMHMM Annotations help

There is no transmembrane helices in POW11835.1.