CAZyme Information: MGYG000002685_00502

Basic Information

• Lineage: Bacteria; Firmicutes_A; Clostridia; Monoglobales_A; UBA9506
• CAZyme ID: MGYG000002685_00502
• CAZy Family: GH105
• CAZyme Description: Unsaturated rhamnogalacturonyl hydrolase YesR

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
347		39426.41	4.4643

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002685	3385444	MAG	Canada	North America

• Gene Location: Start: 12985; End: 14028 Strand: -

Full Sequence      

MEKQQLEEMIDQVVDRTFALDYTWDWPAGIAFYGVARAWEATGRTEYAERVMEWIDKIEA
IGFPPFTVNAVSLGHVLLSLYQLNGEQKYLDLAERMAEYLTHEAARFGDGVLQHTVSQNY
NFPEQAWADTLFMAAYFLVRIGKQTDNNQYFRDGLNQFYWHIEYLQDKKTQLFYHGWDNI
NQNNLSAIHWGRANAWAALTMAETLELLDAFEPMFMELSDALRDQLAALVRVQDGSGFWH
TVVDDPASYLETSASCGIANALAVYDRVNGFPLYKNNYERAFKQLGCIITEQGAVAGVSA
GTAVMHCLEDYRDVPCKRVQGWGQGLALSFLAELYKTACKSGEADMI

Enzyme Prediction     

No EC number prediction in MGYG000002685_00502.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH105	22	336	2.5e-85	0.9668674698795181

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4225	YesR	5.17e-109	1	337	11	352	Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism].
pfam07470	Glyco_hydro_88	3.59e-90	17	337	20	342	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.
cd04791	LanC_SerThrkinase	7.37e-04	8	114	63	189	Lanthionine synthetase C-like domain associated with serine/threonine kinases. Some members of this subgroup lack the zinc binding site and the active site residues, and therefore are most likely inactive. The function of this domain is unknown.
cd04434	LanC_like	0.001	28	177	5	216	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.
pfam07944	Glyco_hydro_127	0.007	34	114	66	171	Beta-L-arabinofuranosidase, GH127. One member of this family, from Bidobacterium longicum, UniProtKB:E8MGH8, has been characterized as an unusual beta-L-arabinofuranosidase enzyme, EC:3.2.1.185. It rleases l-arabinose from the l-arabinofuranose (Araf)-beta1,2-Araf disaccharide and also transglycosylates 1-alkanols with retention of the anomeric configuration. Terminal beta-l-arabinofuranosyl residues have been found in arabinogalactan proteins from a mumber of different plantt species. beta-l-Arabinofuranosyl linkages with 1-4 arabinofuranosides are also found in the sugar chains of extensin and solanaceous lectins, hydroxyproline (Hyp)2-rich glycoproteins that are widely observed in plant cell wall fractions. The critical residue for catalytic activity is Glu-338, in a ET/SCAS sequence context.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
APC40117.1	1.16e-139	2	336	7	337
AEJ61616.1	1.87e-134	1	334	6	335
ADN01768.1	3.53e-132	6	334	11	335
AEI40550.1	3.78e-132	2	334	7	335
AFH61350.1	7.60e-132	2	334	7	335

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PMM_A	2.59e-45	24	333	66	376	ChainA, Putative cytoplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
3QWT_A	1.48e-42	24	333	65	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]
4XUV_A	7.70e-37	22	333	45	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	6.15e-24	9	285	8	298	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	2.04e-21	24	263	39	288	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     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31521	3.45e-126	2	337	7	338	Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR PE=1 SV=1
O34559	1.12e-20	24	263	39	288	Unsaturated rhamnogalacturonyl hydrolase YteR OS=Bacillus subtilis (strain 168) OX=224308 GN=yteR PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as OTHER

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
1.000062	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002685_00502.