CAZyme Information: MGYG000002517_02110

Basic Information

• Species: Roseburia hominis
• Lineage: Bacteria; Firmicutes_A; Clostridia; Lachnospirales; Lachnospiraceae; Roseburia; Roseburia hominis
• CAZyme ID: MGYG000002517_02110
• CAZy Family: GH53
• CAZyme Description: hypothetical protein

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
378	MGYG000002517_1|CGC28	41907.82	3.6031

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002517	3592125	Isolate	United Kingdom	Europe

• Gene Location: Start: 2323270; End: 2324406 Strand: -

Full Sequence      

MVQVGNEISSGILHEDGEIGTDEDFSGLAGLLQSAISGVRDSSASNTKIVLHLDQGGKNE
LYTWFFGGLLEEAPNLDFDVFGLSYYPMWHGTMEGLQYNLNYLATTYDKEVCVVETAYAW
TTEDGDGVGNVFISGDEETGGYPATVEGQFQFMNDLESVILNVPNDKGIGYFYWEPEWVP
VEGGTYASSAGVAYKNDTVTPSNTWDNMTLFNFNGNALESIKVLNQPSENLLTNINFEQN
EVTTSPSGWNVWLSDTTDSNTVKTEYGSAYDGNYKLTFWDDADYSCSIYKTFTNIPNGTY
QFSVWAMTNGDQDVLQLYAKNYGGDELNTTIETSDINWNIFSIDEIVVTNNTLEIGVYSV
AGADDWCNLDMAILRKVE

Enzyme Prediction     

No EC number prediction in MGYG000002517_02110.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH53	1	223	3e-65	0.6023391812865497
CBM61	230	371	2.5e-35	0.9645390070921985

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3867	GanB	6.76e-77	1	225	174	392	Arabinogalactan endo-1,4-beta-galactosidase [Carbohydrate transport and metabolism].
pfam07745	Glyco_hydro_53	1.65e-71	1	224	128	333	Glycosyl hydrolase family 53. This domain belongs to family 53 of the glycosyl hydrolase classification. These enzymes are enzymes are endo-1,4- beta-galactanases (EC:3.2.1.89). The structure of this domain is known and has a TIM barrel fold.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
AEN97255.1	5.72e-287	1	378	1	378
BBF43144.1	9.63e-152	1	378	170	548
ASA20573.1	3.93e-118	1	370	167	537
ACU84283.1	5.77e-109	1	370	180	549
AVM62188.1	5.61e-105	1	370	177	545

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
7OSK_A	4.83e-46	1	223	185	390	ChainA, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230],7OSK_B Chain B, Arabinogalactan endo-1,4-beta-galactosidase [Ignisphaera aggregans DSM 17230]
1R8L_A	2.19e-31	1	223	159	387	Thestructure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1R8L_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis [Bacillus licheniformis],1UR0_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR0_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_A The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],1UR4_B The structure of endo-beta-1,4-galactanase from Bacillus licheniformis in complex with two oligosaccharide products. [Bacillus licheniformis],2CCR_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2CCR_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_A Structure of Beta-1,4-Galactanase [Bacillus licheniformis],2J74_B Structure of Beta-1,4-Galactanase [Bacillus licheniformis]
2GFT_A	1.51e-30	1	223	159	387	ChainA, Glycosyl Hydrolase Family 53 [Bacillus licheniformis],2GFT_B Chain B, Glycosyl Hydrolase Family 53 [Bacillus licheniformis]
1HJS_A	8.34e-23	1	223	129	328	Structureof two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJS_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_A Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_B Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_C Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus],1HJU_D Structure of two fungal beta-1,4-galactanases: searching for the basis for temperature and pH optimum. [Thermothelomyces thermophilus]
1FHL_A	4.13e-22	1	202	130	327	CrystalStructure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 293k [Aspergillus aculeatus],1FOB_A Crystal Structure Of Beta-1,4-galactanase From Aspergillus Aculeatus At 100k [Aspergillus aculeatus],6Q3R_A ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus],6Q3R_B ASPERGILLUS ACULEATUS GALACTANASE [Aspergillus aculeatus]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
P48843	2.64e-47	1	230	133	352	Uncharacterized protein in bgaB 5'region (Fragment) OS=Niallia circulans OX=1397 PE=3 SV=1
Q65CX5	1.72e-30	1	223	184	412	Endo-beta-1,4-galactanase OS=Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / CCUG 7422 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / NRRL NRS-1264 / Gibson 46) OX=279010 GN=ganB PE=1 SV=1
O07013	1.26e-29	1	223	188	416	Endo-beta-1,4-galactanase OS=Bacillus subtilis (strain 168) OX=224308 GN=ganB PE=1 SV=1
Q8X168	2.28e-22	1	179	146	318	Arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus niger OX=5061 GN=galA PE=1 SV=1
A2RB93	3.12e-22	1	179	146	318	Probable arabinogalactan endo-beta-1,4-galactanase A OS=Aspergillus niger (strain CBS 513.88 / FGSC A1513) OX=425011 GN=galA PE=3 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
0.999786	0.000208	0.000010	0.000001	0.000000	0.000008

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002517_02110.