CAZyme Information: MGYG000000424_01949

Basic Information

• Species: CAG-353 sp900768995
• Lineage: Bacteria; Firmicutes_A; Clostridia; Oscillospirales; Ruminococcaceae; CAG-353; CAG-353 sp900768995
• CAZyme ID: MGYG000000424_01949
• CAZy Family: GH113
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
327		37912.67	4.9923

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000000424	2854163	MAG	Sweden	Europe

• Gene Location: Start: 19117; End: 20100 Strand: +

Full Sequence      

MEIKGFTYGWDSHRGMLGTDSAKKSIETMAAMGGNWAALAFAVTQEKFSSTRFGFDYRRT
DTDREIETAIKQLKESGLKVCLKPVLNCEDGTWRANITFPEKEFPVYDENGRLRSYWNEW
FSCYTAFICHYAEIAEYTGCEMLCIGCEMLGTEHKADMWRELIAEVRKVYHGPLVYNTNH
GKEDNVSWFDALDYIGTSAYYPVEKEGGASAEEMTATWEYHKQGLKKTAEKFGKKIIFME
IGCRSARGCAAMPWDFVHREFPRDEDEQANFYESALRAMWNEPYFAGFFWWDWETNLMPE
DRISTDTGFGIHGKKAEKVLTDWYTNK

Enzyme Prediction     

EC	3.2.1.78

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH113	3	320	1.3e-106	0.9901960784313726

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
cd19608	GH113_mannanase-like	2.67e-109	1	324	1	310	Glycoside hydrolase family 113 beta-1,4-mannanase and similar proteins. Mannan endo-1,4-beta mannosidase (E.C 3.2.1.78) randomly cleaves (1->4)-beta-D-mannosidic linkages in mannans, galactomannans and glucomannans and is also called beta-1,4-mannanase, endo-1,4-beta-mannanase, endo-beta-1,4-mannase, beta-mannanase B, beta-1, 4-mannan 4-mannanohydrolase, endo-beta-mannanase, beta-D-mannanase, 1,4-beta-D-mannan mannanohydrolase, and 4-beta-D-mannan mannanohydrolase. (1->4)-beta-linked mannans are polysaccharides with a linear polymer backbone of (1->4)-beta-linked mannose units (in plants and fungi) or alternating mannose and glucose/galactose units (glucomannan in plants and fungi, and galactomannan and galactoglucomannan in plants), such as in the hemicellulose fraction of hard- and softwoods. Complete degradation of mannan requires a series of enzymes, including beta-1,4-mannanase. According to the CAZy database beta-1,4-mannanases are grouped into various glycoside hydrolase (GH) families; GH family 113 beta-1,4-mannanases include mostly bacterial and archaeal sequences.
cd19606	GH113-like	1.11e-87	3	324	2	303	Glycoside hydrolase family 113 beta-mannosidase and similar proteins. Family 113 glycoside hydrolases cleave (1->4)-beta-glycosidic linkages, such as endo-1,4-beta-mannanase. This family also includes TIM-barrel domains found in gene transfer agent proteins.
cd19607	GTA_TIM-barrel-like	0.001	57	283	68	366	Putative glycoside hydrolase TIM-barrel domain in gene transfer agent and similar proteins. This domain is found in the gene transfer agent protein, such as the Rhodobacter capsulatus putative gene transfer agent protein encoded by orfg15. In the purple nonsulfur bacterium Rhodobacter capsulatus, DNA transmission is mediated via an unusual system, a small bacteriophage-like particle called the gene transfer agent (GTA) that transfers random 4.5-kb segments of the producing cell's genome to recipient cells, where allelic replacement occurs.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
ABX41272.1	3.90e-138	1	324	1	319
QNF27001.1	7.32e-132	3	324	6	317
AOZ92031.1	2.50e-130	3	324	7	320
AIQ18672.1	3.01e-128	3	324	6	317
AIQ53005.1	8.59e-128	3	324	6	317

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
4CD6_A	1.22e-79	3	320	13	310	Thestructure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG [Alicyclobacillus acidocaldarius],4CD7_A The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose [Alicyclobacillus acidocaldarius],4CD7_B The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManIFG and beta-1,4-mannobiose [Alicyclobacillus acidocaldarius],4CD8_A The structure of GH113 beta-mannanase AaManA from Alicyclobacillus acidocaldarius in complex with ManMIm [Alicyclobacillus acidocaldarius]
3CIV_A	2.47e-79	3	320	36	333	Crystalstructure of the endo-beta-1,4-mannanase from Alicyclobacillus acidocaldarius [Alicyclobacillus acidocaldarius]
7DV7_A	7.28e-77	3	326	38	342	ChainA, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DV7_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5]
7DVZ_A	7.28e-77	3	326	38	342	ChainA, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DVZ_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DW8_A Chain A, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DW8_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DWA_A Chain A, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DWA_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5]
7DVJ_A	5.80e-76	3	326	38	342	ChainA, Endo-beta-1,4-mannanase [Bacillus sp. N16-5],7DVJ_B Chain B, Endo-beta-1,4-mannanase [Bacillus sp. N16-5]

Swiss-Prot Hits     

has no Swissprot hit.

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
1.000044	0.000000	0.000000	0.000000	0.000000	0.000000

TMHMM  Annotations     

There is no transmembrane helices in MGYG000000424_01949.