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CAZyme Information: APA10035.1

You are here: Home > Sequence: APA10035.1

Basic Information | Genomic context | Full Sequence | Enzyme annotations |  CAZy signature domains |  CDD domains | CAZyme hits | PDB hits | Swiss-Prot hits | SignalP and Lipop annotations | TMHMM annotations

Basic Information help

Species Sclerotinia sclerotiorum
Lineage Ascomycota; Leotiomycetes; ; Sclerotiniaceae; Sclerotinia; Sclerotinia sclerotiorum
CAZyme ID APA10035.1
CAZy Family GH27
CAZyme Description unspecified product
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
889 CP017818|CGC11 95981.22 4.7425
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_Ssclerotiorum1980UF-70 11368 665079 238 11130
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

EC 1.1.3.-:1

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA7 466 690 1.3e-51 0.48253275109170307

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223727 UbiH 1.96e-24 5 407 4 363
2-polyprenyl-6-methoxyphenol hydroxylase and related FAD-dependent oxidoreductases [Coenzyme transport and metabolism, Energy production and conversion].
223354 GlcD 4.05e-21 447 712 2 272
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 5.06e-21 475 611 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.
235980 PRK07236 1.30e-19 1 176 4 166
hypothetical protein; Provisional
411242 urate_HpxO 3.18e-17 5 173 1 166
FAD-dependent urate hydroxylase HpxO. HpxO is an FAD-dependent urate hydroxylase (EC 1.14.13.113). Like the factor independent urate hydroxylase (EC 1.7.3.3), it consumes O2 and converts urate to 5-hydroxyisourate, which decomposes spontaneously to allantoin and CO2. However, HpxO oxidizes NADH to NAD(+), and produces H20, while EC 1.7.3.3 produces H202 as a byproduct.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
8.59e-24 474 887 63 491
3.64e-23 474 887 63 491
3.64e-23 474 887 63 491
4.93e-19 467 712 51 297
7.99e-18 417 878 1 480

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.64e-35 5 376 3 370
Crystal structure of a putative FAD containing monooxygenase from Photorhabdus luminescens subsp. laumondii TTO1 (Target PSI-012791) [Photorhabdus laumondii subsp. laumondii TTO1]
2.94e-24 467 878 37 449
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]
3.93e-24 467 878 37 449
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]
7.02e-24 467 878 37 449
The crystal structure of EncM H138T mutant [Streptomyces maritimus],6FYE_B The crystal structure of EncM H138T mutant [Streptomyces maritimus]
1.25e-23 467 878 37 449
The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_B The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_C The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYB_D The crystal structure of EncM L144M mutant [Streptomyces maritimus],6FYC_A The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus],6FYC_B The crystal structure of EncM L144M mutant complex with dioxygen under 15 bars O2 pressure [Streptomyces maritimus]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
7.07e-92 6 399 493 926
Dual O-methyltransferase/FAD-dependent monooxygenase elcB OS=Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) OX=321614 GN=elcB PE=1 SV=2
7.18e-86 6 390 458 857
Dual O-methyltransferase/FAD-dependent monooxygenase CTB3 OS=Cercospora beticola OX=122368 GN=CTB3 PE=3 SV=1
1.73e-83 6 390 458 857
Dual O-methyltransferase/FAD-dependent monooxygenase CTB3 OS=Cercospora nicotianae OX=29003 GN=CTB3 PE=1 SV=2
4.29e-59 466 887 69 503
FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1
1.62e-57 424 873 5 471
FAD-linked oxidoreductase azaL OS=Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a / NRRL 328 / USDA 3528.7) OX=380704 GN=azaL PE=2 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000062 0.000001

TMHMM  Annotations      help

There is no transmembrane helices in APA10035.1.