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CAZyme Information: MGYG000004223_01824

You are here: Home > Sequence: MGYG000004223_01824

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 UMGS1883 sp900763305
Lineage Bacteria; Firmicutes_A; Clostridia; UMGS1883; UMGS1883; UMGS1883; UMGS1883 sp900763305
CAZyme ID MGYG000004223_01824
CAZy Family GH105
CAZyme Description Unsaturated rhamnogalacturonyl hydrolase YesR
CAZyme Property
Protein Length CGC Molecular Weight Isoelectric Point
348 MGYG000004223_18|CGC1 39469.74 4.5906
Genome Property
Genome Assembly ID Genome Size Genome Type Country Continent
MGYG000004223 2575981 MAG United Kingdom Europe
Gene Location Start: 27317;  End: 28363  Strand: +

Full Sequence      Download help

Enzyme Prediction      help

No EC number prediction in MGYG000004223_01824.

CAZyme Signature Domains help

Family Start End Evalue family coverage
GH105 33 343 6.4e-102 0.9578313253012049

CDD Domains      download full data without filtering help

Cdd ID Domain E-Value qStart qEnd sStart sEnd Domain Description
COG4225 YesR 2.67e-103 33 343 32 348
Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism].
pfam07470 Glyco_hydro_88 7.34e-94 20 343 12 338
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 0.007 46 196 11 157
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
QGQ98394.1 1.32e-132 19 344 25 350
ANY67857.1 2.03e-127 1 344 6 349
ADL35710.1 1.04e-126 34 343 49 359
AIQ43751.1 1.54e-126 6 344 13 350
QUL58446.1 2.18e-126 6 344 13 350

PDB Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
3QWT_A 6.57e-108 5 343 29 375
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 8.85e-106 5 343 30 376
ChainA, Putative cytoplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
4XUV_A 1.62e-90 11 343 17 367
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]
4WU0_A 3.05e-23 33 347 21 359
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]
3K11_A 1.59e-18 103 325 169 392
Crystalstructure of Putative glycosyl hydrolase (NP_813087.1) from BACTEROIDES THETAIOTAOMICRON VPI-5482 at 1.80 A resolution [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits      download full data without filtering help

Hit ID E-Value Query Start Query End Hit Start Hit End Description
O31521 3.68e-56 35 343 29 334
Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1
P0A3U6 5.19e-10 143 324 1 199
Protein Atu3128 OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=Atu3128 PE=3 SV=1
P0A3U7 5.19e-10 143 324 1 199
24.9 kDa protein in picA locus OS=Rhizobium radiobacter OX=358 PE=2 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
1.000064 0.000000 0.000000 0.000000 0.000000 0.000000

TMHMM  Annotations      help

There is no transmembrane helices in MGYG000004223_01824.