CAZyme Information: MGYG000000057_00297

Basic Information

• Species: Bacteroides sp002491635
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides sp002491635
• CAZyme ID: MGYG000000057_00297
• CAZy Family: GH76
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
377	MGYG000000057_2|CGC2	43169.19	4.5627

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000057	4370351	Isolate	United Kingdom	Europe

• Gene Location: Start: 72423; End: 73556 Strand: +

Full Sequence      

MKRILFCLPLLLLALQSCEIEDEYMYDKGGYTIDWEAAADSSSVTLIDRFWNASEHYFNY
GNDGSIKDFHYWPQAHAMDVMIDAYNRTADSKYSDLFDKWYTGIKAKNGGSYWNNFYDDM
EWIALTMIRLYEATDDSKYLQTAQEMWNEIKTGWNDYAGGGIAWTHDQPWSKNACSNGPA
SLIAARLYNINKNEEDLQWALEIYNWEREHLFNPATGAIYDNINGESGEVGSFSLSYNQG
TFLGTAYELYKITKEVSYLKDARKAANFGISNSDMIDTGNNLLRDEGDGDGGLFKGIFMR
YYVQLIMEPGLEPAYKKKFITFFNNNAETLWRKGINKLDLLYSTSWAMNNSGNNHLTTQT
SGCTLIEAKALFEKSLK

Enzyme Prediction     

No EC number prediction in MGYG000000057_00297.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH76	55	352	1.1e-86	0.8379888268156425

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
pfam03663	Glyco_hydro_76	9.78e-53	35	332	2	315	Glycosyl hydrolase family 76. Family of alpha-1,6-mannanases.
COG4833	COG4833	5.49e-48	35	346	3	323	Predicted alpha-1,6-mannanase, GH76 family [Carbohydrate transport and metabolism].
cd04434	LanC_like	4.75e-05	117	346	1	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.
cd04792	LanM-like	0.003	123	267	499	622	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	0.009	123	274	14	142	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
QUU01224.1	1.84e-262	1	377	1	377
QUT37354.1	1.84e-262	1	377	1	377
QQA30005.1	3.72e-262	1	377	1	377
BBK86488.1	3.72e-262	1	377	1	377
QUT65780.1	3.72e-262	1	377	1	377

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
6SHD_A	1.03e-86	34	373	53	390	Structureof the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6],6SHD_B Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6],6SHD_C Structure of the GH76A alpha-1,6-mannanase from Salegentibacter sp. HEL1_6 [Salegentibacter sp. Hel_I_6]
6Y8F_A	3.34e-85	34	373	54	391	ChainA, Alpha-1,6-endo-mannanase GH76A mutant [Salegentibacter sp. Hel_I_6]
6SHM_A	2.66e-84	34	373	54	391	Aninactive (D136A and D137A) variant of alpha-1,6-mannanase, GH76A of Salegentibacter sp. HEL1_6 in complex with alpha-1,6-mannotetrose [Salegentibacter sp. Hel_I_6]
3K7X_A	5.28e-55	67	373	41	341	ChainA, Lin0763 protein [Listeria innocua]
4D4A_A	6.24e-38	23	331	15	325	ChainA, Alpha-1,6-mannanase [Niallia circulans],4D4A_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4B_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4B_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4C_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4C_B Chain B, Alpha-1,6-mannanase [Niallia circulans],4D4D_A Chain A, Alpha-1,6-mannanase [Niallia circulans],4D4D_B Chain B, Alpha-1,6-mannanase [Niallia circulans],5N0F_A Chain A, Alpha-1,6-mannanase [Niallia circulans],5N0F_B Chain B, Alpha-1,6-mannanase [Niallia circulans],6ZBX_A Chain A, Alpha-1,6-mannanase [Niallia circulans],6ZBX_B Chain B, Alpha-1,6-mannanase [Niallia circulans],7NL5_A Chain A, Alpha-1,6-mannanase [Niallia circulans]

Swiss-Prot Hits     

has no Swissprot hit.

SignalP and Lipop Annotations

This protein is predicted as LIPO

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.000002	0.001503	0.998560	0.000000	0.000001	0.000001

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000057_00297.