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CAZyme Information: QVM13434.1

You are here: Home > Sequence: QVM13434.1

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 Coccidioides posadasii
Lineage Ascomycota; Eurotiomycetes; ; Onygenaceae; Coccidioides; Coccidioides posadasii
CAZyme ID QVM13434.1
CAZy Family GT71
CAZyme Description FAD-binding PCMH-type domain-containing protein [Source:UniProtKB/TrEMBL;Acc:E9DE51]
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
586 CP075072|CGC1 65885.99 6.8541
Genome Property
Genome Version/Assembly ID Genes Strain NCBI Taxon ID Non Protein Coding Genes Protein Coding Genes
FungiDB-61_CposadasiiSilveira2022 8438 N/A 139 8299
Gene Location

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in QVM13434.1.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 41 569 2.7e-164 0.9904214559386973

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
223354 GlcD 3.48e-33 57 558 1 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
396238 FAD_binding_4 9.31e-31 94 232 2 139
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.
397178 FAD-oxidase_C 3.98e-13 428 557 120 247
FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.
183043 PRK11230 2.89e-10 44 292 14 244
glycolate oxidase subunit GlcD; Provisional
178402 PLN02805 2.59e-09 54 270 98 302
D-lactate dehydrogenase [cytochrome]

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
0.0 1 586 1 586
5.46e-158 37 566 27 560
7.49e-154 42 575 35 573
2.47e-153 37 567 26 560
3.39e-152 37 566 30 564

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3.38e-116 42 566 5 522
Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXD_B Crystal structure of eugenol oxidase in complex with isoeugenol [Rhodococcus jostii RHA1],5FXE_A Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXE_B Crystal structure of eugenol oxidase in complex with coniferyl alcohol [Rhodococcus jostii RHA1],5FXF_A Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXF_B Crystal structure of eugenol oxidase in complex with benzoate [Rhodococcus jostii RHA1],5FXP_A Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1],5FXP_B Crystal structure of eugenol oxidase in complex with vanillin [Rhodococcus jostii RHA1]
9.00e-102 42 565 12 553
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum]
2.51e-101 42 565 12 553
STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum],1W1J_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: The505Ser Mutant [Penicillium simplicissimum]
2.51e-101 42 565 12 553
Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1DZN_B Asp170Ser mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]
2.51e-101 42 565 12 553
Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum],1E0Y_B Structure of the D170S/T457E double mutant of vanillyl-alcohol oxidase [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1.82e-100 42 565 12 553
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
1.85e-99 41 560 8 515
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
1.92e-15 54 281 35 252
Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
2.23e-14 81 277 29 218
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
1.19e-12 54 299 13 246
D-lactate dehydrogenase OS=Anaerostipes hadrus OX=649756 GN=CL2_23160 PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI CS Position
1.000075 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in QVM13434.1.