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CAZyme Information: MGYG000004680_01935

You are here: Home > Sequence: MGYG000004680_01935

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
Lineage Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Lacrimispora;
CAZyme ID MGYG000004680_01935
CAZy Family GH105
CAZyme Description Unsaturated rhamnogalacturonyl hydrolase YesR
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
349 MGYG000004680_24|CGC1 40001.58 4.9414
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004680 3596809 MAG Germany Europe
Gene Location Start: 40311;  End: 41360  Strand: -

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004680_01935.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH105 24 335 1.5e-79 0.963855421686747

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4225 YesR 4.03e-93 1 338 6 350
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism].
pfam07470 Glyco_hydro_88 2.52e-72 22 335 20 337
Glycosyl Hydrolase Family 88. Unsaturated glucuronyl hydrolase catalyzes the hydrolytic release of unsaturated glucuronic acids from oligosaccharides (EC:3.2.1.-) produced by the reactions of polysaccharide lyases.
cd04434 LanC_like 1.63e-05 10 161 26 185
Cyclases involved in the biosynthesis of lantibiotics, and similar proteins. LanC is the cyclase enzyme of the lanthionine synthetase. Lanthionine is a lantibiotic, a unique class of peptide antibiotics. They are ribosomally synthesized as a precursor peptide and then post-translationally modified to contain thioether cross-links called lanthionines (Lans) or methyllanthionines (MeLans), in addition to 2,3-didehydroalanine (Dha) and (Z)-2,3-didehydrobutyrine (Dhb). These unusual amino acids are introduced by the dehydration of serine and threonine residues, followed by thioether formation via addition of cysteine thiols, catalysed by LanB and LanC or LanM. LanC, the cyclase component, is a zinc metalloprotein, whose bound metal has been proposed to activate the thiol substrate for nucleophilic addition. A related domain is also present in LanM and other pro- and eukaryotic proteins with poorly characterized functions.

CAZyme Hits      help

Hit ID E-Value Query Start Query End Hit Start Hit End
BCJ94220.1 1.16e-212 1 349 1 349
QEI31009.1 1.83e-209 1 349 1 349
QHB23517.1 1.83e-209 1 349 1 349
AOZ97580.1 1.80e-186 1 349 1 349
ADL32982.1 1.80e-186 1 349 1 349

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
4XUV_A 7.89e-31 29 337 47 366
Crystalstructure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris [Thermothielavioides terrestris NRRL 8126],4XUV_B Crystal structure of a glycoside hydrolase family 105 (GH105) enzyme from Thielavia terrestris [Thermothielavioides terrestris NRRL 8126]
3QWT_A 8.97e-31 29 317 65 357
ChainA, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_B Chain B, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_C Chain C, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A],3QWT_D Chain D, Putative GH105 family protein [Salmonella enterica subsp. enterica serovar Paratyphi A]
3PMM_A 1.61e-28 29 317 66 358
ChainA, Putative cytoplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4WU0_A 8.94e-17 16 286 10 288
StructuralAnalysis of C. acetobutylicum ATCC 824 Glycoside Hydrolase From Family 105 [Clostridium acetobutylicum ATCC 824],4WU0_B Structural Analysis of C. acetobutylicum ATCC 824 Glycoside Hydrolase From Family 105 [Clostridium acetobutylicum ATCC 824]
1NC5_A 3.56e-08 29 293 39 316
Structureof Protein of Unknown Function of YteR from Bacillus Subtilis [Bacillus subtilis],2D8L_A Crystal Structure of Unsaturated Rhamnogalacturonyl Hydrolase in complex with dGlcA-GalNAc [Bacillus subtilis]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31521 1.04e-105 1 337 1 335
Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1
O34559 1.95e-07 29 293 39 316
Unsaturated rhamnogalacturonyl hydrolase YteR OS=Bacillus subtilis (strain 168) OX=224308 GN=yteR PE=1 SV=1
L7P9J4 3.47e-06 30 298 59 340
Unsaturated 3S-rhamnoglycuronyl hydrolase OS=Nonlabens ulvanivorans OX=906888 GN=IL45_01505 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
1.000038 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004680_01935.