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CAZyme Information: ACLA_094140-t26_1-p1

You are here: Home > Sequence: ACLA_094140-t26_1-p1

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 Aspergillus clavatus
Lineage Ascomycota; Eurotiomycetes; ; Aspergillaceae; Aspergillus; Aspergillus clavatus
CAZyme ID ACLA_094140-t26_1-p1
CAZy Family GT4
CAZyme Description FAD binding domain protein
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
463 DS027052|CGC6 49102.39 5.5777
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_AclavatusNRRL1 9428 344612 287 9141
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 42 458 2.6e-88 0.962882096069869

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 1.11e-31 9 455 1 451
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 9.61e-31 44 177 3 139
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 2.60e-19 39 198 63 231
cytokinin dehydrogenase
223882 MurB 4.63e-14 41 256 20 222
UDP-N-acetylenolpyruvoylglucosamine reductase [Cell wall/membrane/envelope biogenesis].
273750 pln_FAD_oxido 2.68e-10 34 127 24 122
plant-specific FAD-dependent oxidoreductase. This model represents an uncharacterized plant-specific family of FAD-dependent oxidoreductases. At least seven distinct members are found in Arabidopsis thaliana. The family shows considerable sequence similarity to three different enzymes of ascorbic acid biosynthesis: L-galactono-1,4-lactone dehydrogenase (EC 1.3.2.3) from higher plants, D-arabinono-1,4-lactone oxidase (EC 1.1.3.37 from Saccharomyces cerevisiae, and L-gulonolactone oxidase (EC 1.1.3.8) from mouse, as well as to a bacterial sorbitol oxidase. The class of compound acted on by members of this family is unknown.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
1.78e-31 9 454 28 484
6.55e-27 39 455 60 484
1.26e-26 45 455 67 489
1.26e-26 45 455 67 489
2.32e-26 45 455 67 489

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.30e-63 22 461 25 460
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]
7.00e-63 22 461 25 460
Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_B Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_C Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],4XLO_D Crystal Structure of EncM (crystallized with 4 mM NADPH) [Streptomyces maritimus],6FOQ_A The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_B The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_C The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOQ_D The crystal structure of EncM complexed with dioxygen under 15 bar of oxygen pressure. [Streptomyces maritimus],6FOW_A The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_B The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_C The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FOW_D The crystal structure of EncM complexed with dioxygen under 10 bar of oxygen pressure. [Streptomyces maritimus],6FP3_A The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_B The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_C The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FP3_D The crystal structure of EncM complexed with dioxygen under 5 bar of oxygen pressure. [Streptomyces maritimus],6FY8_A The crystal structure of EncM bromide soak [Streptomyces maritimus],6FY9_A The crystal structure of EncM complex with xenon under 15 bars Xe pressure [Streptomyces maritimus],6FYA_A The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus],6FYA_B The crystal structure of EncM under anaerobic conditions [Streptomyces maritimus]
7.69e-63 22 461 29 464
The crystal structure of EncM [Streptomyces maritimus],3W8W_B The crystal structure of EncM [Streptomyces maritimus],3W8X_A The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8X_B The complex structure of EncM with trifluorotriketide [Streptomyces maritimus],3W8Z_A The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus],3W8Z_B The complex structure of EncM with hydroxytetraketide [Streptomyces maritimus]
9.80e-63 22 461 25 460
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]
1.37e-62 22 461 25 460
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
5.55e-128 7 456 1 445
FAD-linked oxidoreductase pyvE OS=Aspergillus violaceofuscus (strain CBS 115571) OX=1450538 GN=pyvE PE=3 SV=1
2.37e-46 19 454 24 441
FAD-linked oxidoreductase DDB_G0289697 OS=Dictyostelium discoideum OX=44689 GN=DDB_G0289697 PE=2 SV=1
3.27e-44 25 461 61 503
FAD-linked oxidoreductase OXR1 OS=Magnaporthe oryzae (strain 70-15 / ATCC MYA-4617 / FGSC 8958) OX=242507 GN=OXR1 PE=1 SV=1
3.29e-39 16 461 48 496
FAD-linked oxidoreductase srdI OS=Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987) OX=367110 GN=srdI PE=2 SV=1
2.25e-38 19 454 15 447
(R)-6-hydroxynicotine oxidase OS=Paenarthrobacter nicotinovorans OX=29320 GN=6-hdno PE=1 SV=2

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000057 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in ACLA_094140-t26_1-p1.