CAZyme Information: MGYG000002281_03559

Basic Information

• Species: Bacteroides faecis
• Lineage: Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Bacteroidaceae; Bacteroides; Bacteroides faecis
• CAZyme ID: MGYG000002281_03559
• CAZy Family: GH2
• CAZyme Description: Exo-beta-D-glucosaminidase

CAZyme Property

Protein Length	CGC	Molecular Weight	Isoelectric Point
903	MGYG000002281_21|CGC1	103228.75	7.0859

Genome Property

Genome Assembly ID	Genome Size	Genome Type	Country	Continent
MGYG000002281	6145961	Isolate	China	Asia

• Gene Location: Start: 31351; End: 34062 Strand: +

Full Sequence      

MHNFVKTLFSVLLLFFCSVLTAQNRMNDARDPNRIWLDSEVTHHGDYQWKMMKAGDTTDP
GEKISSSDYPTEKWLPAIVPGTVLNSLVYNQKYPEPYYGVNNKIESKLIPDISQVGRDFY
TYWFRTEFAVPQSFKGKNVWLQLDGINYRAEVWVNGNLLSTVNGMFIQDYINVTDFVKIG
KNNALAVKVYPVDVPGSTKPKSWGAAGEFHNGGNGNIGLNTTMLMTVGWDFTFMDGIRDR
NTGIWKNISIYATGKVALRHPFIKSELRKPDYDQARETVSVEVINSSTSNSGINCKVKGE
IVGENISFEKSFRVIRGEQKLVTFSPEEFPQLVMNSPRLWWPVNKGPQNLYDLKLTVSVD
GVICDSVKTRFGIREITSDTKTPDKSRVFYVNGKRLFIRGTNWIPEAMLRHSDERTYAEL
RYTRQSGVNLLRMWGGGIAESDYFFQLCDELGLLVWQEFWMTGDTRHPHDKALYMSNVES
TVKRIRNHPSLAYYVASNESTEMTGTPELLNQLDGTRGYQMQSECAGVHDGSPYKQVNPM
QHYENTASPRGSRVDGFNPEYGAPTLPTVEILREMMDEKDLWPINKEVWDYLDGNGFHLM
TTMYTDLVNHYGKSSSIDEFAQKGQLLGAINSKSIWEVWNYNKLDYGDRFCSGLLFWYHN
CSMRQVASRMWDWSLEPTASLYHTANSLEPLHAQFDYLKNTVSVVNDFYRSFDNYKVTAQ
VYDINSRKVFEESAAVNLPADGVANDALTIRFPDGISQVHFIKLILKDEKGKEISSNFYW
RSNDKYEGKTTLTGPAASGFEDLSKLRASKVKLAYKVREEGDNYFVDITMRNTSNQIAFF
NQLQFLNAKMSPIRPSFYTDNFFSLTPGEKKTVTIETAKEKLSEGAMLVLKGWNIDSQKY
KLK

Enzyme Prediction     

No EC number prediction in MGYG000002281_03559.

CAZyme Signature Domains

Family	Start	End	Evalue	family coverage
GH2	48	740	7.5e-86	0.6715425531914894

CDD Domains     

Cdd ID	Domain	E-Value	qStart	qEnd	sStart	sEnd	Domain Description
COG3250	LacZ	2.88e-37	111	550	53	462	Beta-galactosidase/beta-glucuronidase [Carbohydrate transport and metabolism].
pfam18368	Ig_GlcNase	8.89e-21	777	895	1	104	Exo-beta-D-glucosaminidase Ig-fold domain. This domain can be found in 2 glycoside hydrolase subfamily of beta-glucosaminidases (EC:3.2.1.165) such as CsxA, from Amycolatopsis orientalis that has exo-beta-D-glucosaminidase (exo-chitosanase) activity. It has an immunoglobulin-like topology.
PRK10150	PRK10150	6.63e-19	123	499	68	417	beta-D-glucuronidase; Provisional
PRK10340	ebgA	2.45e-18	124	500	113	450	cryptic beta-D-galactosidase subunit alpha; Reviewed
pfam00703	Glyco_hydro_2	5.21e-16	256	374	1	106	Glycosyl hydrolases family 2. This family contains beta-galactosidase, beta-mannosidase and beta-glucuronidase activities.

CAZyme Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End
QUT40873.1	0.0	1	903	1	903
ALJ39811.1	0.0	1	903	1	903
QUT73024.1	0.0	1	903	1	903
BCA52194.1	0.0	26	903	1	878
QDH53380.1	0.0	1	903	1	903

PDB Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
5N6U_A	4.58e-57	72	895	41	830	Crystalstructure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_B Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_C Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12],5N6U_D Crystal structure of Beta-D-Mannosidase from Dictyoglomus thermophilum. [Dictyoglomus thermophilum H-6-12]
2JE8_A	3.89e-44	51	884	1	827	Structureof a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482],2JE8_B Structure of a beta-mannosidase from Bacteroides thetaiotaomicron [Bacteroides thetaiotaomicron VPI-5482]
7OP6_A	3.91e-44	51	884	1	827	ChainA, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP6_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_A Chain A, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482],7OP7_B Chain B, Beta-mannosidase [Bacteroides thetaiotaomicron VPI-5482]
2VJX_A	6.83e-44	59	884	12	825	Structuraland biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VJX_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VL4_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VMF_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VO5_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VOT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron VPI-5482],2VQT_A Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VQT_B Structural and biochemical evidence for a boat-like transition state in beta-mannosidases [Bacteroides thetaiotaomicron],2VR4_A Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482],2VR4_B Transition-state mimicry in mannoside hydrolysis: characterisation of twenty six inhibitors and insight into binding from linear free energy relationships and 3-D structure [Bacteroides thetaiotaomicron VPI-5482]
2WBK_A	1.62e-43	59	884	12	825	Structureof the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482],2WBK_B Structure of the Michaelis complex of beta-mannosidase, Man2A, provides insight into the conformational itinerary of mannoside hydrolysis [Bacteroides thetaiotaomicron VPI-5482]

Swiss-Prot Hits     

Hit ID	E-Value	Query Start	Query End	Hit Start	Hit End	Description
Q75W54	1.42e-110	46	894	10	935	Mannosylglycoprotein endo-beta-mannosidase OS=Arabidopsis thaliana OX=3702 GN=EBM PE=1 SV=3
Q5H7P5	5.99e-97	46	900	7	950	Mannosylglycoprotein endo-beta-mannosidase OS=Lilium longiflorum OX=4690 GN=EBM PE=1 SV=4
Q82NR8	2.12e-79	49	898	57	899	Exo-beta-D-glucosaminidase OS=Streptomyces avermitilis (strain ATCC 31267 / DSM 46492 / JCM 5070 / NBRC 14893 / NCIMB 12804 / NRRL 8165 / MA-4680) OX=227882 GN=csxA PE=1 SV=1
Q4R1C4	5.53e-52	49	870	38	863	Exo-beta-D-glucosaminidase OS=Hypocrea jecorina OX=51453 GN=gls93 PE=1 SV=1
D4AUH1	2.43e-49	29	898	21	880	Exo-beta-D-glucosaminidase ARB_07888 OS=Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) OX=663331 GN=ARB_07888 PE=1 SV=1

SignalP and Lipop Annotations

This protein is predicted as SP

Other	SP_Sec_SPI	LIPO_Sec_SPII	TAT_Tat_SPI	TATLIP_Sec_SPII	PILIN_Sec_SPIII
0.001152	0.872880	0.125166	0.000257	0.000263	0.000255

TMHMM  Annotations     

There is no transmembrane helices in MGYG000002281_03559.