logo
sublogo
You are browsing environment: HUMAN GUT
help

CAZyme Information: MGYG000001044_00343

You are here: Home > Sequence: MGYG000001044_00343

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 Campylobacter sp900753405
Lineage Bacteria; Campylobacterota; Campylobacteria; Campylobacterales; Campylobacteraceae; Campylobacter; Campylobacter sp900753405
CAZyme ID MGYG000001044_00343
CAZy Family AA4
CAZyme Description 4-cresol dehydrogenase [hydroxylating] flavoprotein subunit
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
518 MGYG000001044_11|CGC1 58558.64 9.2363
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000001044 1440385 MAG Denmark Europe
Gene Location Start: 50029;  End: 51585  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000001044_00343.

CAZyme Signature Domains help

Family Start End Evalue family coverage
AA4 3 516 1.7e-206 0.9865900383141762

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
pfam01565 FAD_binding_4 1.85e-30 55 195 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.
COG0277 GlcD 4.20e-29 21 509 1 455
FAD/FMN-containing dehydrogenase [Energy production and conversion].
PRK11230 PRK11230 3.05e-14 13 304 14 288
glycolate oxidase subunit GlcD; Provisional
PLN02805 PLN02805 2.26e-13 54 254 133 323
D-lactate dehydrogenase [cytochrome]
pfam02913 FAD-oxidase_C 4.14e-10 407 508 145 247
FAD linked oxidases, C-terminal domain. This domain has a ferredoxin-like fold.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
CCD51118.1 1.51e-143 4 517 29 578
ATZ45204.1 6.02e-143 4 517 29 578
APA07334.1 8.00e-143 4 517 29 578
QSZ30937.1 2.34e-136 4 517 29 578
AFJ11909.1 7.79e-134 4 511 7 543

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
1WVE_A 3.00e-217 6 514 8 517
p-CresolMethylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVE_B p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida],1WVF_A p-Cresol Methylhydroxylase: Alteration of the Structure of the Flavoprotein Subunit upon its Binding to the Cytochrome Subunit [Pseudomonas putida]
1DII_A 3.11e-217 6 514 9 518
ChainA, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DII_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_A Chain A, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida],1DIQ_B Chain B, P-CRESOL METHYLHYDROXYLASE [Pseudomonas putida]
5FXD_A 1.43e-134 5 511 4 516
Crystalstructure 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]
1E0Y_A 1.67e-130 4 511 10 548
Structureof 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]
1W1L_A 2.36e-130 4 511 10 548
STRUCTUREOF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum],1W1L_B STRUCTURE OF THE OCTAMERIC FLAVOENZYME VANILLYL-ALCOHOL OXIDASE: Phe454Tyr Mutant [Penicillium simplicissimum]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
P09788 1.70e-216 6 514 9 518
4-cresol dehydrogenase [hydroxylating] flavoprotein subunit OS=Pseudomonas putida OX=303 GN=pchF PE=1 SV=3
P56216 5.15e-129 4 511 10 548
Vanillyl-alcohol oxidase OS=Penicillium simplicissimum OX=69488 GN=VAOA PE=1 SV=1
F1QXM5 6.25e-17 13 250 30 258
Probable D-lactate dehydrogenase, mitochondrial OS=Danio rerio OX=7955 GN=ldhd PE=2 SV=1
P94535 7.42e-17 54 272 40 247
Glycolate oxidase subunit GlcD OS=Bacillus subtilis (strain 168) OX=224308 GN=glcD PE=3 SV=1
Q94AX4 2.13e-13 54 508 145 559
D-lactate dehydrogenase [cytochrome], mitochondrial OS=Arabidopsis thaliana OX=3702 GN=DLD PE=1 SV=1

SignalP and Lipop Annotations help

This protein is predicted as OTHER

Other SP_Sec_SPI LIPO_Sec_SPII TAT_Tat_SPI TATLIP_Sec_SPII PILIN_Sec_SPIII
1.000053 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000001044_00343.