CAZyme Information: MGYG000002651_02114

Basic Information

• Species: Faecalibacterium sp900772565
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; Faecalibacterium; Faecalibacterium sp900772565
• CAZyme ID: MGYG000002651_02114
• CAZy Family: GH105
• CAZyme Description: Unsaturated rhamnogalacturonyl hydrolase YteR

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
349	MGYG000002651_119|CGC1	40758.39	5.4842

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002651	2281803	MAG	United Republic of Tanzania	Africa

• Gene Location: Start: 4; End: 1053 Strand: +

Full Sequence      

MRSGKPNKWNYIDGCMITACLSLYKTTGDEKYLEFSKEFIDYFVQPDGSIKTYDPKEYNL
DNVNQGKNLFILYDIYGDEKYRKAIDTIRSQLLTQPRTKEGNFWHKDIYPWQVWLDGTYM
AQPFYMEYETRFNKMQGCIDSYKQFMNIKKHMRDEKTGLYYHGYDESRQMYWADPETGCS
PNFWLRAMGWFLVAMVDVLERMDEQLYNEYRGIMAMLKQTVEDMHKFQDEQTGMFWQVID
HPEAEGNYLETSGTALFAYAVLKGVRLGYLPKRMAAWAEKAFYGTCDRYLSKNPDGSLQL
DGICLVAGLGGKDHRDGSLAYYFSEPVVCNDAKGVGPLVLAYTEMIARK

Enzyme Prediction     

No EC number prediction in MGYG000002651_02114.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH105	5	346	4.5e-113	0.9698795180722891

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4225	YesR	2.96e-96	2	345	26	353	Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism].
pfam07470	Glyco_hydro_88	4.47e-80	7	349	25	343	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	0.001	19	112	108	210	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	0.003	23	88	187	254	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.
pfam03663	Glyco_hydro_76	0.010	6	42	214	250	Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
CBL00657.1	4.93e-272	1	349	33	381
AXB29657.1	2.01e-271	1	349	33	381
AXA82451.1	6.91e-263	1	349	33	381
CBK99741.1	2.81e-262	1	349	33	381
ATP00557.1	1.63e-261	1	349	33	381

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4WU0_A	5.79e-107	9	344	23	357	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	1.97e-77	7	345	37	364	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]
2GH4_A	8.29e-77	7	345	27	354	ChainA, Putative glycosyl hydrolase yteR [Bacillus subtilis]
3QWT_A	7.37e-14	9	298	65	338	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	1.82e-12	143	284	178	319	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O34559	1.08e-76	7	345	37	364	Unsaturated rhamnogalacturonyl hydrolase YteR OS=Bacillus subtilis (strain 168) OX=224308 GN=yteR PE=1 SV=1
P0A3U6	6.17e-43	120	346	1	229	Protein Atu3128 OS=Agrobacterium fabrum (strain C58 / ATCC 33970) OX=176299 GN=Atu3128 PE=3 SV=1
P0A3U7	6.17e-43	120	346	1	229	24.9 kDa protein in picA locus OS=Rhizobium radiobacter OX=358 PE=2 SV=1
O31521	4.25e-16	9	276	29	285	Unsaturated rhamnogalacturonyl hydrolase YesR OS=Bacillus subtilis (strain 168) OX=224308 GN=yesR 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
1.000056	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002651_02114.