CAZyme Information: MGYG000003402_03509

Basic Information

• Species: Paenibacillus lactis
• Lineage: Bacteria; Firmicutes; Bacilli; Paenibacillales; Paenibacillaceae; Paenibacillus; Paenibacillus lactis
• CAZyme ID: MGYG000003402_03509
• CAZy Family: GH105
• CAZyme Description: Unsaturated rhamnogalacturonyl hydrolase YesR

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
343	MGYG000003402_1192|CGC1	38388.41	4.7847

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000003402	5924245	MAG	United States	North America

• Gene Location: Start: 200; End: 1231 Strand: -

Full Sequence      

MPALVFDEQYIGQVMDKVVERTFRMDFSWDWPGGVAFYGVCEAYEATGKMEYLEQLKSWV
DENMEDGLPKLSVNGVSIGHSLLTLYNVYGDERYIETAKEMAEYLTHDAVRFGEGIFQHT
VNSEAYNFPEQAWVDTMFMAGYFLLRIGALLGRDDYFEDGLRQYHGHENCLQDPVTNLYY
HGWDNIAGNHMSGVFWCRGNAWAALTMARALELVPVTHPSFMIIEGSLRDQLSSLVRLQH
ESGLWHTITTDPQSPLETSGSAGIATALLTKGRIYNKYTQKSIDGILTKITEDGTVTGVS
AGTAVMKNAAGYIGVPDKRIQGWGQGLTLAFLAEVLKVKNNPY

Enzyme Prediction     

No EC number prediction in MGYG000003402_03509.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH105	25	337	4.2e-88	0.9728915662650602

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG4225	YesR	1.96e-131	1	337	6	351	Rhamnogalacturonyl hydrolase YesR [Carbohydrate transport and metabolism].
pfam07470	Glyco_hydro_88	4.61e-111	9	337	7	341	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	7.88e-08	32	294	54	306	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.
cd04792	LanM-like	1.00e-05	33	199	549	711	Cyclases involved in the biosynthesis of class II lantibiotics, and similar proteins. LanM-like proteins. LanM is a bifunctional enzyme, involved in the synthesis of class II lantibiotics. It is responsible for both the dehydration and the cyclization of the precursor-peptide during lantibiotic synthesis. The C-terminal domain shows similarity to LanC, the cyclase component of the lan operon, but the N terminus seems to be unrelated to the dehydratase, LanB.
pfam05147	LANC_like	7.20e-05	33	282	60	288	Lanthionine synthetase C-like protein. Lanthionines are thioether bridges that are putatively generated by dehydration of Ser and Thr residues followed by addition of cysteine residues within the peptide. This family contains the lanthionine synthetase C-like proteins 1 and 2 which are related to the bacterial lanthionine synthetase components C (LanC). LANCL1 (P40 seven-transmembrane-domain protein) and LANCL2 (testes-specific adriamycin sensitivity protein) are thought to be peptide-modifying enzyme components in eukaryotic cells. Both proteins are produced in large quantities in the brain and testes and may have role in the immune surveillance of these organs. Lanthionines are found in lantibiotics, which are peptide-derived, post-translationally modified antimicrobials produced by several bacterial strains. This region contains seven internal repeats.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ANY76695.1	1.23e-252	1	343	1	343
ACX66563.1	2.24e-239	1	343	1	343
AYB43328.1	2.62e-238	1	343	1	343
QOT11242.1	5.28e-238	1	343	1	343
AWP30837.1	1.39e-233	1	343	1	343

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
3PMM_A	4.11e-39	29	337	66	379	ChainA, Putative cytoplasmic protein [Klebsiella pneumoniae subsp. pneumoniae MGH 78578]
3QWT_A	2.17e-37	14	337	40	378	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	7.17e-35	29	334	47	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]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
O31521	1.30e-177	1	343	1	343	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
1.000058	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000003402_03509.